| Year |
Citation |
Score |
| 2013 |
Peng D, Ogura H, Ma LH, Evans JP, de Montellano PR, La Mar GN. Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt. Journal of Inorganic Biochemistry. 121: 179-86. PMID 23391487 DOI: 10.1016/J.Jinorgbio.2013.01.004 |
0.765 |
|
| 2012 |
Peng D, Ma LH, Smith KM, Zhang X, Sato M, La Mar GN. Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study. Biochemistry. 51: 7054-63. PMID 22913621 DOI: 10.1021/Bi3007803 |
0.743 |
|
| 2011 |
Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN. Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study. Biochemistry. 50: 8823-33. PMID 21870860 DOI: 10.1021/Bi200978G |
0.734 |
|
| 2010 |
Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN. Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. Journal of Inorganic Biochemistry. 104: 1063-70. PMID 20655112 DOI: 10.1016/J.Jinorgbio.2010.06.003 |
0.476 |
|
| 2010 |
Peng D, Ma LH, Ogura H, Yang EC, Zhang X, Yoshida T, La Mar GN. 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: implications for product release. Biochemistry. 49: 5832-40. PMID 20540495 DOI: 10.1021/Bi1000867 |
0.721 |
|
| 2009 |
Peng D, Ogura H, Zhu W, Ma LH, Evans JP, Ortiz de Montellano PR, La Mar GN. Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase. Biochemistry. 48: 11231-42. PMID 19842713 DOI: 10.1021/Bi901216S |
0.735 |
|
| 2009 |
Ogura H, Evans JP, Peng D, Satterlee JD, Ortiz de Montellano PR, La Mar GN. The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism. Biochemistry. 48: 3127-37. PMID 19243105 DOI: 10.1021/Bi802360G |
0.742 |
|
| 2009 |
Ma LH, Liu Y, Zhang X, Yoshida T, La Mar GN. 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure. Journal of Inorganic Biochemistry. 103: 10-9. PMID 18976815 DOI: 10.1016/j.jinorgbio.2008.08.012 |
0.667 |
|
| 2008 |
Ogura H, Evans JP, de Montellano PR, La Mar GN. Implication for using heme methyl hyperfine shifts as indicators of heme seating as related to stereoselectivity in the catabolism of heme by heme oxygenase: in-plane heme versus axial his rotation. Biochemistry. 47: 421-30. PMID 18078349 DOI: 10.1021/bi7017333 |
0.361 |
|
| 2007 |
La Mar GN. Application of the paramagnetic dipole field for solution NMR active site structure determination in low-spin, cyanide-inhibited ferric hemoproteins. Iubmb Life. 59: 513-27. PMID 17701546 DOI: 10.1080/15216540701194121 |
0.376 |
|
| 2006 |
Liu Y, Ma LH, Zhang X, Yoshida T, Satterlee JD, La Mar GN. 1H NMR Study of the influence of hemin vinyl-->methyl substitution on the interaction between the C-terminus and substrate and the "aging" of the heme oxygenase from Neisseria meningitidis: induction of active site structural heterogeneity by a two-fold symmetric hemin. Biochemistry. 45: 13875-88. PMID 17105206 DOI: 10.1021/bi061747q |
0.671 |
|
| 2006 |
Bondarenko V, Dewilde S, Moens L, La Mar GN. Solution 1H NMR characterization of the axial bonding of the two His in oxidized human cytoglobin. Journal of the American Chemical Society. 128: 12988-99. PMID 17002396 DOI: 10.1021/Ja063330D |
0.434 |
|
| 2006 |
Ma LH, Liu Y, Zhang X, Yoshida T, La Mar GN. 1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network. Journal of the American Chemical Society. 128: 6657-68. PMID 16704267 DOI: 10.1021/ja0584626 |
0.682 |
|
| 2006 |
Ma LH, Liu Y, Zhang X, Yoshida T, Langry KC, Smith KM, La Mar GN. Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules. Journal of the American Chemical Society. 128: 6391-9. PMID 16683803 DOI: 10.1021/Ja0578505 |
0.657 |
|
| 2006 |
Liu Y, Ma LH, Zhang X, Yoshida T, Satterlee JD, La Mar GN. Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure. Biochemistry. 45: 3875-86. PMID 16548515 DOI: 10.1021/bi0523097 |
0.612 |
|
| 2006 |
Zhu W, Li Y, Wang J, Ortiz de Montellano PR, La Mar GN. Solution NMR study of environmental effects on substrate seating in human heme oxygenase: influence of polypeptide truncation, substrate modification and axial ligand. Journal of Inorganic Biochemistry. 100: 97-107. PMID 16337271 DOI: 10.1016/j.jinorgbio.2005.08.010 |
0.361 |
|
| 2005 |
Xia Z, Nguyen BD, Brunori M, Cutruzzolà F, La Mar GN. 1H-NMR study of the effect of temperature through reversible unfolding on the heme pocket molecular structure and magnetic properties of aplysia limacina cyano-metmyoglobin. Biophysical Journal. 89: 4149-58. PMID 16150970 DOI: 10.1529/biophysj.105.062398 |
0.384 |
|
| 2005 |
Liu Y, Zhang X, Yoshida T, La Mar GN. Solution 1H NMR characterization of the distal H-bond network and the effective axial field in the resting-state, high-spin ferric, substrate-bound complex of heme oxygenase from N. meningitidis. Journal of the American Chemical Society. 127: 6409-22. PMID 15853349 DOI: 10.1021/ja042339h |
0.707 |
|
| 2005 |
Bondarenko V, Wang J, Kalish H, Balch AL, La Mar GN. Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I incorporated into the active site of cyano-metmyoglobin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 283-93. PMID 15821940 DOI: 10.1007/S00775-005-0640-X |
0.517 |
|
| 2004 |
Tran AT, Kolczak U, La Mar GN. Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin. Biochimica Et Biophysica Acta. 1701: 75-87. PMID 15450177 DOI: 10.1016/J.Bbapap.2004.06.003 |
0.721 |
|
| 2004 |
Liu Y, Zhang X, Yoshida T, La Mar GN. 1H NMR characterization of the solution active site structure of substrate-bound, cyanide-inhibited heme oxygenase from Neisseria meningitidis: comparison to crystal structures. Biochemistry. 43: 10112-26. PMID 15287739 DOI: 10.1021/bi049438s |
0.695 |
|
| 2004 |
Li Y, Syvitski RT, Auclair K, de Montellano PR, La Mar GN. 1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex. The Journal of Biological Chemistry. 279: 10195-205. PMID 14660632 DOI: 10.1074/Jbc.M308379200 |
0.459 |
|
| 2003 |
Li Y, Syvitski RT, Auclair K, Ortiz de Montellano P, La Mar GN. Solution 1H, 15N NMR spectroscopic characterization of substrate-bound, cyanide-inhibited human heme oxygenase: water occupation of the distal cavity. Journal of the American Chemical Society. 125: 13392-403. PMID 14583035 DOI: 10.1021/Ja036176T |
0.388 |
|
| 2003 |
Tran AT, Kolczak U, La Mar GN. Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated alpha-chain from human hemoglobin A. Biochimica Et Biophysica Acta. 1650: 59-72. PMID 12922170 DOI: 10.1016/S1570-9639(03)00202-4 |
0.727 |
|
| 2003 |
Ma D, Musto R, Smith KM, La Mar GN. Solution NMR characterization of the electronic structure and magnetic properties of high-spin ferrous heme in deoxy myoglobin from Aplysia limacina. Journal of the American Chemical Society. 125: 8494-504. PMID 12848555 DOI: 10.1021/Ja035256U |
0.3 |
|
| 2003 |
Du W, Syvitski R, Dewilde S, Moens L, La Mar GN. Solution 1h NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin. Journal of the American Chemical Society. 125: 8080-1. PMID 12837059 DOI: 10.1021/Ja034584R |
0.371 |
|
| 2003 |
Du W, Xia Z, Dewilde S, Moens L, La Mar GN. 1H NMR study of the molecular structure and magnetic properties of the active site for the cyanomet complex of O2-avid hemoglobin from the trematode Paramphistomum epiclitum. European Journal of Biochemistry / Febs. 270: 2707-20. PMID 12823541 DOI: 10.1046/J.1432-1033.2003.03638.X |
0.452 |
|
| 2003 |
Sulc F, Fleischer E, Farmer PJ, Ma D, La Mar GN. 1H NMR structure of the heme pocket of HNO-myoglobin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 348-52. PMID 12589571 DOI: 10.1007/s00775-002-0422-7 |
0.405 |
|
| 2003 |
Li Y, Syvitski RT, Chu GC, Ikeda-Saito M, La Mar GN. Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae Journal of Biological Chemistry. 278: 6651-6663. PMID 12480929 DOI: 10.1074/Jbc.M211249200 |
0.467 |
|
| 2002 |
Syvitski RT, Li Y, Auclair K, Ortiz De Montellano PR, La Mar GN. 1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1. Journal of the American Chemical Society. 124: 14296-7. PMID 12452690 DOI: 10.1021/Ja028108X |
0.374 |
|
| 2002 |
Sham S, Calzolai L, Wang PL, Bren K, Haarklau H, Brereton PS, Adams MW, La Mar GN. A solution NMR molecular model for the aspartate-ligated, cubane cluster containing ferredoxin from the hyperthermophilic archeaon Pyrococcus furiosus. Biochemistry. 41: 12498-508. PMID 12369841 DOI: 10.1021/bi020347 |
0.645 |
|
| 2002 |
de Ropp JS, Sham S, Asokan A, Newmyer S, Ortiz de Montellano PR, La Mar GN. Influence of the distal his in imparting imidazolate character to the proximal his in heme peroxidase: (1)h NMR spectroscopic study of cyanide-inhibited his42-->ala horseradish peroxidase. Journal of the American Chemical Society. 124: 11029-37. PMID 12224950 DOI: 10.1021/ja020176w |
0.46 |
|
| 2002 |
Li Y, Syvitski RT, Auclair K, Wilks A, Ortiz De Montellano PR, La Mar GN. Solution NMR characterization of an unusual distal H-bond network in the active site of the cyanide-inhibited, human heme oxygenase complex of the symmetric substrate, 2,4-dimethyldeuterohemin. The Journal of Biological Chemistry. 277: 33018-31. PMID 12070167 DOI: 10.1074/Jbc.M204216200 |
0.422 |
|
| 2001 |
Webba da Silva M, Sham S, Gorst CM, Calzolai L, Brereton PS, Adams MW, La Mar GN. Solution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties for the hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus. Biochemistry. 40: 12575-83. PMID 11601981 DOI: 10.1021/bi0106179 |
0.381 |
|
| 2001 |
Hu B, Hauksson JB, Tran AT, Kolczak U, Pandey RK, Rezzano IN, Smith KM, La Mar GN. 1H and 13C NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins. Journal of the American Chemical Society. 123: 10063-70. PMID 11592885 DOI: 10.1021/Ja011175R |
0.744 |
|
| 2001 |
Wang J, Li Y, Ma D, Kalish H, Balch AL, La Mar GN. Solution NMR determination of the seating(s) of meso-nitro-etioheme-1 in myoglobin: implications for steric constraints to meso position access in heme degradation by coupled oxidation. Journal of the American Chemical Society. 123: 8080-8. PMID 11506564 DOI: 10.1021/ja010651a |
0.526 |
|
| 2001 |
La Mar GN, Kolczak U, Tran AT, Chien EY. Solution 1H NMR characterization of axial interactions of the proximal and distal His in the cyanomet complexes of the isolated chains and the 65 kDa intact tetramer of human hemoglobin A. Journal of the American Chemical Society. 123: 4266-74. PMID 11457193 DOI: 10.1021/ja004168w |
0.355 |
|
| 2001 |
Asokan A, de Ropp JS, Newmyer SL, Ortiz de Montellano PR, La Mar GN. Solution 1H NMR of the molecular and electronic structure of the heme cavity and substrate binding pocket of high-spin ferric horseradish peroxidase: effect of His42Ala mutation. Journal of the American Chemical Society. 123: 4243-54. PMID 11457190 DOI: 10.1021/ja003687w |
0.415 |
|
| 2001 |
La Mar GN, Asokan A, Espiritu B, Yeh DC, Auclair K, Ortiz De Montellano PR. Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form. The Journal of Biological Chemistry. 276: 15676-87. PMID 11297521 DOI: 10.1074/Jbc.M009974200 |
0.399 |
|
| 2000 |
Tran AT, Kalish H, Balch AL, La Mar GN. Solution 1H NMR investigation of the seating and rotational "hopping" of centrosymmetric etioheme-I in myoglobin: effect of globin origin and its oxidation/spin state on heme dynamics. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 624-33. PMID 11085653 DOI: 10.1007/S007750000145 |
0.76 |
|
| 2000 |
Xia Z, Nguyen BD, La Mar GN. The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: implication for structure determination/refinement in paramagnetic metalloproteins. Journal of Biomolecular Nmr. 17: 167-74. PMID 10921780 DOI: 10.1023/A:1008309121949 |
0.303 |
|
| 2000 |
Yeh DC, Thorsteinsson MV, Bevan DR, Potts M, La Mar GN. Solution 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune. Biochemistry. 39: 1389-99. PMID 10684619 DOI: 10.1021/Bi992081L |
0.399 |
|
| 2000 |
Nguyen BD, Xia Z, Cutruzzolá F, Allocatelli CT, Brunori M, La Mar GN. Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin. The Journal of Biological Chemistry. 275: 742-51. PMID 10625603 DOI: 10.1074/jbc.275.2.742 |
0.43 |
|
| 1999 |
Xia Z, Zhang W, Nguyen BD, La Mar GN, Kloek AP, Goldberg DE. 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin Journal of Biological Chemistry. 274: 31819-31826. PMID 10542205 DOI: 10.1074/Jbc.274.45.31819 |
0.46 |
|
| 1999 |
Wang PL, Calzolai L, Bren KL, Teng Q, Jenney FE, Brereton PS, Howard JB, Adams MW, La Mar GN. Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity. Biochemistry. 38: 8167-78. PMID 10387062 DOI: 10.1021/Bi990241N |
0.653 |
|
| 1999 |
de Ropp JS, Mandal PK, La Mar GN. Solution 1H NMR investigation of the heme cavity and substrate binding site in cyanide-inhibited horseradish peroxidase. Biochemistry. 38: 1077-86. PMID 9894004 DOI: 10.1021/bi982125a |
0.4 |
|
| 1999 |
Kolczak U, Hauksson JB, Davis NL, Pande U, De Ropp JS, Langry KC, Smith KM, La Mar GN. 1H NMR investigation of the role of intrinsic heme versus protein- induced rhombic perturbations on the electronic structure of low-spin ferrihemoproteins: Effect of heme substituents on heme orientation in myoglobin Journal of the American Chemical Society. 121: 835-843. DOI: 10.1021/ja983045x |
0.357 |
|
| 1998 |
Wu Y, Chien EY, Sligar SG, La Mar GN. Influence of proximal side mutations on the molecular and electronic structure of cyanomet myoglobin: an 1H NMR study. Biochemistry. 37: 6979-90. PMID 9578585 DOI: 10.1021/Bi9728295 |
0.457 |
|
| 1998 |
Nguyen BD, Zhao X, Vyas K, La Mar GN, Lile RA, Brucker EA, Phillips GN, Olson JS, Wittenberg JB. Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata. The Journal of Biological Chemistry. 273: 9517-26. PMID 9545280 DOI: 10.1074/Jbc.273.16.9517 |
0.343 |
|
| 1998 |
Gorst CM, Wilks A, Yeh DC, Ortiz De Montellano PR, La Mar GN. Solution 1H NMR investigation of the molecular and electronic structure of the active site of substrate-bound human heme oxygenase: The nature of the distal hydrogen bond donor to bound ligands Journal of the American Chemical Society. 120: 8875-8884. DOI: 10.1021/ja9815475 |
0.389 |
|
| 1998 |
Bougault CM, Dou Y, Ikeda-Saito M, Langry KC, Smith KM, La Mar GN. Solution 1H NMR study of the electronic structure and magnetic properties of high-spin ferrous or deoxy myoglobins Journal of the American Chemical Society. 120: 2113-2123. DOI: 10.1021/ja973197c |
0.35 |
|
| 1997 |
Zhang W, Cutruzzolá F, Allocatelli CT, Brunori M, La Mar GN. A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: elucidation of the distal hydrogen bonding network by solution NMR. Biophysical Journal. 73: 1019-30. PMID 9251819 DOI: 10.1016/S0006-3495(97)78135-9 |
0.352 |
|
| 1997 |
Calzolai L, Gorst CM, Bren KL, Zhou ZH, Adams MWW, La Mar GN. Solution NMR study of the electronic structure and magnetic properties of cluster ligation mutants of the four-iron ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus Journal of the American Chemical Society. 119: 9341-9350. DOI: 10.1021/Ja9715455 |
0.608 |
|
| 1996 |
Wu Y, Basti M, Gambacurta A, Chiancone E, Ascoli F, La Mar GN. Proton-NMR investigation of the heme cavity in the cyanomet derivative of the cooperative homodimeric hemoglobin from Scapharca inaequivalvis. Biochimica Et Biophysica Acta. 1298: 261-75. PMID 8980651 DOI: 10.1016/S0167-4838(96)00137-9 |
0.426 |
|
| 1996 |
Wang PL, Donaire A, Zhou ZH, Adams MW, La Mar GN. Molecular model of the solution structure for the paramagnetic four-iron ferredoxin from the hyperthermophilic archaeon Thermococcus litoralis. Biochemistry. 35: 11319-28. PMID 8784186 DOI: 10.1021/bi960783u |
0.312 |
|
| 1996 |
Donaire A, Zhou ZH, Adams MM, La Mar GN. 1H NMR investigation of the secondary structure, tertiary contacts and cluster environment of the four-iron ferredoxin from the hyperthermophilic archaeon Thermococcus litoralis. Journal of Biomolecular Nmr. 7: 35-47. PMID 8720830 DOI: 10.1007/BF00190455 |
0.349 |
|
| 1996 |
Zhang W, La Mar GN, Gersonde K. Solution 1H-NMR structure of the heme cavity in the low-affinity state for the allosteric monomeric cyano-met hemoglobins from Chironomus thummi thummi. Comparison to the crystal structure. European Journal of Biochemistry / Febs. 237: 841-53. PMID 8647133 |
0.402 |
|
| 1996 |
Clark K, Dugad LB, Bartsch RG, Cusanovich MA, La Mar GN. An interpretive basis of the proton nuclear magnetic resonance hyperfine shifts for structure determination of high-spin ferric hemoproteins. Implications for the reversible thermal unfolding of ferricytochrome c′ from Rhodopseudomonas palustris Journal of the American Chemical Society. 118: 4654-4664. |
0.306 |
|
| 1995 |
Gorst CM, Yeh YH, Teng Q, Calzolai L, Zhou ZH, Adams MW, La Mar GN. 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure. Biochemistry. 34: 600-10. PMID 7819255 |
0.346 |
|
| 1995 |
De Ropp JS, Chen Z, La Mar GN. Identification of residues in the aromatic substrate binding site of horseradish peroxidase by 1H NMR studies on isozymes Biochemistry. 34: 13477-13484. PMID 7577936 |
0.325 |
|
| 1995 |
Calzolai L, Gorst CM, Zhao ZH, Teng Q, Adams MW, La Mar GN. 1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states. Biochemistry. 34: 11373-84. PMID 7547865 |
0.315 |
|
| 1994 |
Qin J, La Mar GN, Dou Y, Admiraal SJ, Ikeda-Saito M. 1H NMR study of the solution molecular and electronic structure of engineered distal myoglobin His64(E7) Val/Val68(E11) His double mutant. Coordination of His64(E11) at the sixth position in both low-spin and high-spin states. The Journal of Biological Chemistry. 269: 1083-90. PMID 8288565 |
0.361 |
|
| 1994 |
Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN. Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage. Biochemistry. 33: 6631-41. PMID 8204600 DOI: 10.1021/Bi00187A033 |
0.41 |
|
| 1994 |
Teng Q, Zhou ZH, Smith ET, Busse SC, Howard JB, Adams MW, La Mar GN. Solution 1H NMR determination of secondary structure for the three-iron form of ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus. Biochemistry. 33: 6316-26. PMID 8193147 |
0.405 |
|
| 1994 |
Lee KB, McLachlan SJ, La Mar GN. Hydrogen isotope effects on the proton nuclear magnetic resonance spectrum of bovine ferricytochrome b5: axial hydrogen bonding involving the axial His-39 imidazole ligand. Biochimica Et Biophysica Acta. 1208: 22-30. PMID 8086435 DOI: 10.1016/0167-4838(94)90155-4 |
0.415 |
|
| 1994 |
La Mar GN, Dalichow F, Zhao X, Dou Y, Ikeda-Saito M, Chiu ML, Sligar SG. 1H NMR investigation of distal mutant deoxy myoglobins. Interpretation of proximal His contact shifts in terms of a localized distal water molecule. The Journal of Biological Chemistry. 269: 29629-35. PMID 7961951 |
0.326 |
|
| 1994 |
Donaire A, Gorst CM, Zhou ZH, Adams MWW, La Mar GN. 1H NMR investigation of the electronic structure of the four-iron ferredoxin from the hyperthermophilic archaeon Thermococcus litoralis Journal of the American Chemical Society. 116: 6841-6849. |
0.321 |
|
| 1993 |
Rajarathnam K, Qin J, La Mar GN, Chiu ML, Sligar SG. Solution structure determination of the heme cavity in the E7 His-->Val cyano-met myoglobin point mutant based on the 1H NMR detected dipolar field of the iron: evidence for contraction of the heme pocket. Biochemistry. 32: 5670-80. PMID 8504086 DOI: 10.1021/Bi00072A024 |
0.309 |
|
| 1993 |
Lee KB, La Mar GN, Mansfield KE, Smith KM, Pochapsky TC, Sligar SG. Interpretation of hyperfine shift patterns in ferricytochromes b5 in terms of angular position of the heme: a sensitive probe for peripheral heme protein interactions. Biochimica Et Biophysica Acta. 1202: 189-99. PMID 8399380 DOI: 10.1016/0167-4838(93)90004-B |
0.418 |
|
| 1993 |
Qin J, La Mar GN, Ascoli F, Brunori M. Solution nuclear magnetic resonance determination of active site structure for a paramagnetic protein: cyanomet Aplysia myoglobin. Journal of Molecular Biology. 231: 1009-23. PMID 8390582 DOI: 10.1006/jmbi.1993.1348 |
0.433 |
|
| 1993 |
Qin J, La Mar GN, Cutruzzolá F, Allocatelli CT, Brancaccio A, Brunori M. Solution 1H nuclear magnetic resonance determination of the distal pocket structure of cyanomet complexes of genetically engineered sperm whale myoglobin His64 (E7)-->Val, Thr67 (E10)-->Arg. The role of distal hydrogen bonding by Arg67 (E10) in modulating ligand tilt. Biophysical Journal. 65: 2178-90. PMID 8298042 DOI: 10.1016/S0006-3495(93)81270-0 |
0.325 |
|
| 1993 |
Qin J, Pande U, La Mar GN, Ascoli F, Ascenzi P, Cutruzzolá F, Travaglini-Allocatelli C, Brunori M. 1H NMR study of the dynamics of the pH modulation of axial coordination in Aplysia limacina (Val(E7)) and sperm whale double mutant His(E7)-->Val,Thr(E10)-->Arg metmyoglobin. The Journal of Biological Chemistry. 268: 24012-21. PMID 8226945 |
0.329 |
|
| 1992 |
Qin J, La Mar GN, Ascoli F, Bolognesi M, Brunori M. Solution 1H nuclear magnetic resonance determination of hydrogen bonding of the E10 (66) Arg side-chain to the bound ligand in Aplysia cyano-met myoglobin. Journal of Molecular Biology. 224: 891-7. PMID 1569577 DOI: 10.1016/0022-2836(92)90456-T |
0.319 |
|
| 1992 |
Qin J, La Mar GN. Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin. Journal of Biomolecular Nmr. 2: 597-618. PMID 1490108 DOI: 10.1007/BF02192849 |
0.391 |
|
| 1992 |
Busse SC, La Mar GN, Yu LP, Howard JB, Smith ET, Zhou ZH, Adams MW. Proton NMR investigation of the oxidized three-iron clusters in the ferredoxins from the hyperthermophilic archae Pyrococcus furiosus and Thermococcus litoralis. Biochemistry. 31: 11952-62. PMID 1445925 DOI: 10.1021/Bi00162A038 |
0.357 |
|
| 1992 |
Banci L, Dugad LB, La Mar GN, Keating KA, Luchinat C, Pierattelli R. 1H nuclear magnetic resonance investigation of cobalt(II) substituted carbonic anhydrase. Biophysical Journal. 63: 530-43. PMID 1420895 DOI: 10.1016/S0006-3495(92)81607-7 |
0.4 |
|
| 1992 |
La Mar GN, Hernández G, de Ropp JS. H NMR investigation of the influence of interacting sites on the dynamics and thermodynamics of substrate and ligand binding to horseradish peroxidase. Biochemistry. 31: 9158-68. PMID 1390702 |
0.369 |
|
| 1992 |
Chatfield MJ, La Mar GN. 1H nuclear magnetic resonance study of the prosthetic group in sulfhemoglobin. Archives of Biochemistry and Biophysics. 295: 289-96. PMID 1316736 DOI: 10.1016/0003-9861(92)90520-7 |
0.424 |
|
| 1992 |
Rajarathnam K, La Mar GN, Chiu ML, Sligar SG. Determination of the orientation of the magnetic axes of the cyano-MetMb complexes of point mutants of myoglobin by solution 1H NMR: Influence of his E7 → Gly and Arg CD3 → Gly substitutions Journal of the American Chemical Society. 114: 9048-9058. |
0.325 |
|
| 1992 |
Keating KA, La Mar GN, Shiau FY, Smith KM. 1H NMR study of the molecular and electronic structure of paramagnetic iron chlorin complexes of myoglobin: Dynamic heterogeneity of the heme pocket Journal of the American Chemical Society. 114: 6513-6520. |
0.358 |
|
| 1991 |
Wu JZ, La Mar GN, Yu LP, Lee KB, Walker FA, Chiu ML, Sligar SG. 1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation. Biochemistry. 30: 2156-65. PMID 1998676 DOI: 10.1021/Bi00222A020 |
0.412 |
|
| 1991 |
Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM. 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Biochemistry. 30: 1878-87. PMID 1993202 DOI: 10.1021/Bi00221A021 |
0.425 |
|
| 1991 |
de Ropp JS, La Mar GN, Wariishi H, Gold MH. NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase. The Journal of Biological Chemistry. 266: 15001-8. PMID 1869537 |
0.463 |
|
| 1991 |
de Ropp JS, Yu LP, La Mar GN. 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase. Journal of Biomolecular Nmr. 1: 175-90. PMID 1841693 DOI: 10.1007/BF01877229 |
0.4 |
|
| 1991 |
Busse SC, La Mar GN, Howard JB. Two-dimensional NMR investigation of iron-sulfur cluster electronic and molecular structure of oxidized Clostridium pasteurianum ferredoxin. Interpretability of contact shifts in terms of cysteine orientation. The Journal of Biological Chemistry. 266: 23714-23. PMID 1748648 |
0.415 |
|
| 1991 |
Peyton DH, La Mar GN, Ramaprasad S, Unger SW, Sankar S, Gersonde K. Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi thummi cyanomet hemoglobins. Dynamic stability of the heme pocket as monitored by labile proton exchange. Journal of Molecular Biology. 221: 1015-26. PMID 1658331 DOI: 10.1016/0022-2836(91)80189-2 |
0.398 |
|
| 1991 |
Medforth CJ, Shiau FY, La Mar GN, Smith KM. Very long-range isotope shifts in the proton NMR spectra of deuteriated haemins Journal of the Chemical Society, Chemical Communications. 590-592. DOI: 10.1039/C39910000590 |
0.301 |
|
| 1991 |
Keating KA, De Ropp JS, La Mar GN, Balch AL, Shiau FY, Smith KM. Assignment by 2D NMR bond correlation spectroscopy of hyperfine-shifted and strongly relaxed protons in iron porphyrin and chlorin complexes Inorganic Chemistry. 30: 3258-3263. |
0.389 |
|
| 1991 |
Rajarathnam K, La Mar GN, Chiu ML, Sligar SG, Singh JP, Smith KM. 1H NMR Hyperfine Shift Pattern as a Probe for Ligation State in High-Spin Ferric Hemoproteins: Water Binding in Metmyoglobin Mutants Journal of the American Chemical Society. 113: 7886-7892. |
0.32 |
|
| 1991 |
La Mar GN, Hauksson JB, Dugad LB, Liddell PA, Venkataramana N, Smith KM. Proton NMR study of the heme rotational mobility in myoglobin: The role of propionate salt bridges in anchoring the heme Journal of the American Chemical Society. 113: 1544-1550. |
0.314 |
|
| 1990 |
Emerson SD, La Mar GN. NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand. Biochemistry. 29: 1556-66. PMID 2334714 |
0.402 |
|
| 1990 |
Donald Emerson S, La Mar GN. Solution structural characterization of cyanometmyoglobin: Resonance assignment of heme cavity residues by two-dimensional NMR Biochemistry. 29: 1545-1556. PMID 2334713 |
0.397 |
|
| 1990 |
Yu LP, La Mar GN, Mizukami H. Rearrangement of the distal pocket accompanying E7 His----Gln substitution in elephant carbonmonoxy- and oxymyoglobin: 1H NMR identification of a new aromatic residue in the heme pocket. Biochemistry. 29: 2578-85. PMID 2334682 |
0.312 |
|
| 1990 |
Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG. 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. Biochemistry. 29: 9623-31. PMID 2271605 DOI: 10.1021/Bi00493A017 |
0.333 |
|
| 1990 |
Hauksson JB, La Mar GN, Pande U, Pandey RK, Parish DW, Singh JP, Smith KM. 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers. Biochimica Et Biophysica Acta. 1041: 186-94. PMID 2265204 DOI: 10.1016/0167-4838(90)90064-M |
0.401 |
|
| 1990 |
Dugad LB, La Mar GN, Lee HC, Ikeda-Saito M, Booth KS, Caughey WS. A nuclear Overhauser effect study of the active site of myeloperoxidase. Structural similarity of the prosthetic group to that on lactoperoxidase. The Journal of Biological Chemistry. 265: 7173-9. PMID 2158989 |
0.41 |
|
| 1990 |
Dugad LB, La Mar GN, Banci L, Bertini I. Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effect. Biochemistry. 29: 2263-71. PMID 2110829 DOI: 10.1021/Bi00461A009 |
0.365 |
|
| 1990 |
Yu LP, La Mar GN, Rajarathnam K. 1H NMR resonance assignment of the active site residues of paramagnetic proteins by 2D bond correlation spectroscopy: Metcyanomyoglobin Journal of the American Chemical Society. 112: 9527-9534. |
0.388 |
|
| 1990 |
Arasasingham RD, Balch AL, Cornman CR, De Ropp JS, Eguchi K, La Mar GN. 1H NMR studies of iron(III) porphyrins with axial phenoxide or thiophenoxide ligands Inorganic Chemistry. 29: 1847-1850. |
0.32 |
|
| 1990 |
Hauksson JB, La Mar GN, Pandey RK, Rezzano IN, Smith KM. 1H NMR study of the role of individual heme propionates in modulating structural and dynamic properties of the heme pocket in myoglobin Journal of the American Chemical Society. 112: 6198-6205. |
0.313 |
|
| 1989 |
La Mar GN, Thanabal V, Johnson RD, Smith KM, Parish DW. Deuterium NMR study of structural and dynamic properties of horseradish peroxidase. The Journal of Biological Chemistry. 264: 5428-34. PMID 2925611 |
0.377 |
|
| 1989 |
La Mar GN, Smith WS, Davis NL, Budd DL, Levy MJ. Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin. Biochemical and Biophysical Research Communications. 158: 462-8. PMID 2916994 DOI: 10.1016/S0006-291X(89)80070-1 |
0.328 |
|
| 1989 |
McGourty JL, La Mar GN, Smith KM, Ascoli F, Chiancone E, Pandey RK, Singh JP. Nuclear-magnetic-resonance investigation of the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis. Molecular and electronic structure of the cyano-met derivative. European Journal of Biochemistry / Febs. 184: 53-61. PMID 2776770 DOI: 10.1111/J.1432-1033.1989.Tb14989.X |
0.385 |
|
| 1989 |
Parker WO, Chatfield MJ, La Mar GN. Determination of the chirality of the saturated pyrrole in sulfmyoglobin using the nuclear Overhauser effect. Biochemistry. 28: 1517-25. PMID 2719915 |
0.331 |
|
| 1989 |
Lecomte JT, Smit JD, Winterhalter KH, La Mar GN. Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin. Journal of Molecular Biology. 209: 235-47. PMID 2555518 DOI: 10.1016/0022-2836(89)90275-1 |
0.403 |
|
| 1989 |
Thanabal V, La Mar GN. A nuclear Overhauser effect investigation of the molecular and electronic structure of the heme crevice in lactoperoxidase. Biochemistry. 28: 7038-44. PMID 2554963 |
0.379 |
|
| 1989 |
Peyton DH, La Mar GN, Pande U, Ascoli F, Smith KM, Pandey RK, Parish DW, Bolognesi M, Brunori M. Proton nuclear magnetic resonance study of the molecular and electronic structure of the heme cavity in Aplysia cyanometmyoglobin. Biochemistry. 28: 4880-7. PMID 2548594 |
0.401 |
|
| 1989 |
Yamamoto Y, La Mar GN. Proton NMR investigation of the influence of subunit assembly on the low-spin in equilibrium high-spin equilibrium of met-azido hemoglobin A. Biochimica Et Biophysica Acta. 996: 187-94. PMID 2546603 DOI: 10.1016/0167-4838(89)90246-X |
0.335 |
|
| 1989 |
Licoccia S, Chatfield MJ, La Mar GN, Smith KM, Mansfield KE, Anderson RR. Proton NMR study of the molecular and electronic structure of ferric chlorin complexes: Evidence for π bonding by the orbital derived from the porphyrin a1u orbital Journal of the American Chemical Society. 111: 6087-6093. |
0.343 |
|
| 1988 |
Chatfield MJ, La Mar GN, Smith KM, Leung HK, Pandey RK. Identification of the altered pyrrole in the isomeric sulfmyoglobins: hyperfine shift patterns as indicators of ring saturation in ferric chlorins. Biochemistry. 27: 1500-7. PMID 3365403 DOI: 10.1021/Bi00405A016 |
0.366 |
|
| 1988 |
Peyton DH, La Mar GN, Gersonde K. A nuclear Overhauser study of heme orientational isomerism in monomeric Chironomus hemoglobins Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 954: 82-94. PMID 3358941 DOI: 10.1016/0167-4838(88)90058-1 |
0.35 |
|
| 1988 |
La Mar GN, Jue T, Nagai K, Smith KM, Yamamoto Y, Kauten RJ, Thanabal V, Langry KC, Pandey RK, Leung HK. 1H-NMR heme resonance assignments by selective deuteration in low-spin complexes of ferric hemoglobin A. Biochimica Et Biophysica Acta. 952: 131-41. PMID 3337821 DOI: 10.1016/0167-4838(88)90108-2 |
0.635 |
|
| 1988 |
McLachlan SJ, La Mar GN, Lee KB. One- and two-dimensional nuclear Overhauser effect studies of the eletronic/molecular structure of the heme cavity of ferricytochrome b5 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 957: 430-445. PMID 3196721 DOI: 10.1016/0167-4838(88)90234-8 |
0.397 |
|
| 1988 |
Thanabal V, La Mar GN, de Ropp JS. A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidine Biochemistry. 27: 5400-5407. PMID 3179262 |
0.364 |
|
| 1988 |
La Mar GN, Chatfield MJ, Peyton DH, de Ropp JS, Smith WS, Krishnamoorthi R, Satterlee JD, Erman JE. Solvent isotope effects on NMR spectral parameters in high-spin ferric hemoproteins: an indirect probe for distal hydrogen bonding. Biochimica Et Biophysica Acta. 956: 267-76. PMID 2844271 DOI: 10.1016/0167-4838(88)90143-4 |
0.392 |
|
| 1988 |
Donald Emerson S, Lecomte JTJ, La Mar GN. 1H NMR resonance assignment and dynamic analysis of phenylalanine CD1 in a low-spin ferric complex of sperm whale myoglobin Journal of the Chemical Society. 110: 4176-4182. |
0.308 |
|
| 1987 |
Sankar SS, La Mar GN, Smith KM, Fujinari EM. 13C-NMR study of labeled vinyl groups in paramagnetic myoglobin derivatives Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 912: 220-229. PMID 3828362 DOI: 10.1016/0167-4838(87)90092-6 |
0.419 |
|
| 1987 |
Lecomte JT, La Mar GN, Smit JD, Winterhalter KH, Smith KM, Langry KC, Leung HK. Structural and electronic properties of the liver fluke hemoglobin heme cavity by nuclear magnetic resonance: hemin isotope labeling. Journal of Molecular Biology. 197: 101-10. PMID 3681990 DOI: 10.1016/0022-2836(87)90612-7 |
0.344 |
|
| 1987 |
Chatfield MJ, La Mar GN, Kauten RJ. Proton NMR characterization of isomeric sulfmyoglobins: preparation, interconversion, reactivity patterns, and structural features. Biochemistry. 26: 6939-50. PMID 3427054 |
0.41 |
|
| 1987 |
Peyton DH, Krishnamoorthi R, La Mar GN, Gersonde K, Smith KM, Parish DW. Protein-structural heterogeneity in a non-allosteric monomeric insect hemoglobin monitored by proton magnetic resonance spectroscopy European Journal of Biochemistry. 168: 377-383. PMID 2822413 DOI: 10.1111/J.1432-1033.1987.Tb13430.X |
0.311 |
|
| 1987 |
Thanabal V, De Ropp JS, La Mar GN. 1H NMR study of the electronic and molecular structure of the heme cavity in horseradish peroxidase. Complete heme resonance assignments based on saturation transfer and nuclear overhauser effects Journal of the American Chemical Society. 109: 265-272. |
0.356 |
|
| 1987 |
Lecomte JTJ, La Mar GN. 1H NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: Isotope effect on heme electronic structure of myoglobin Journal of the American Chemical Society. 109: 7219-7220. |
0.388 |
|
| 1986 |
Chatfield MJ, La Mar GN, Balch AL, Lecomte JT. Multiple forms of sulfmyoglobin as detected by 1H nuclear magnetic resonance spectroscopy. Biochemical and Biophysical Research Communications. 135: 309-15. PMID 3954774 DOI: 10.1016/0006-291X(86)90978-2 |
0.545 |
|
| 1986 |
McLachlan SJ, La Mar GN, Burns PD, Smith KM, Langry KC. 1H-NMR assignments and the dynamics of interconversion of the isomeric forms of cytochrome b5 in solution Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 874: 274-284. PMID 3790573 DOI: 10.1016/0167-4838(86)90026-9 |
0.304 |
|
| 1986 |
Pande U, La Mar GN, Lecomte JTJ, Ascoli F, Brunori M, Smith KM, Pandey RK, Parish DW, Thanabal V. NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear overhauser effect measurements Biochemistry. 25: 5638-5646. PMID 3778878 DOI: 10.1021/Bi00367A044 |
0.417 |
|
| 1986 |
Yamamoto Y, La Mar GN. 1H NMR study of dynamics and thermodynamics of heme rotational disorder in native and reconstituted hemoglobin A Biochemistry. 25: 5288-5297. PMID 3768348 |
0.359 |
|
| 1986 |
Chatfield MJ, La Mar GN, Balch AL, Smith KM, Parish DW, LePage TJ. Proton NMR study of the influence of heme vinyl groups on the formation of the isomeric forms of sulfmyoglobin. Febs Letters. 206: 343-6. PMID 3758356 DOI: 10.1016/0014-5793(86)81009-2 |
0.447 |
|
| 1986 |
Lecomte JTJ, La Mar GN. The homonuclear Overhauser effect in H2O solution of low-spin hemeproteins - Assignment of protons in the heme cavity of sperm whale myoglobin European Biophysics Journal. 13: 373-381. PMID 3019654 DOI: 10.1007/BF00265673 |
0.348 |
|
| 1985 |
Lecomte JTJ, La Mar GN. 1H NMR study of labile proton exchange in the heme cavity as a probe for the potential ligand entry channel in myoglobin Biochemistry. 24: 7388-7395. PMID 4084588 |
0.366 |
|
| 1985 |
Levy MJ, La Mar GN, Jue T, Smith KM, Pandey RK, Smith WS, Livingston DJ, Brown WD. Proton NMR study of yellowfin tuna myoglobin in whole muscle and solution. Evidence for functional metastable protein forms involving heme orientational disorder. The Journal of Biological Chemistry. 260: 13694-8. PMID 4055753 |
0.55 |
|
| 1985 |
La Mar GN, Yamamoto Y, Jue T, Smith KM, Pandey RK. 1H NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin. Biochemistry. 24: 3826-31. PMID 4052368 DOI: 10.1021/Bi00336A002 |
0.61 |
|
| 1985 |
Lecomte JT, Johnson RD, La Mar GN. Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effects. Biochimica Et Biophysica Acta. 829: 268-74. PMID 2986702 DOI: 10.1016/0167-4838(85)90197-9 |
0.335 |
|
| 1985 |
Unger SW, Jue T, La Mar GN. Proton NMR dipolar relaxation by delocalized spin density in low-spin ferric porphyrin complexes Journal of Magnetic Resonance (1969). 61: 448-456. DOI: 10.1016/0022-2364(85)90185-4 |
0.571 |
|
| 1985 |
Balch AL, Chan YW, La Mar GN, Latos-Grazynski L, Renner MW. Proton and deuterium nuclear magnetic resonance studies on iron(II) complexes of N-substituted porphyrins Inorganic Chemistry. 24: 1437-1443. |
0.306 |
|
| 1984 |
Krishnamoorthi R, La Mar GN, Mizukami H, Romero A. A 1H NMR comparison of the met-cyano complexes of elephant and sperm whale myoglobin. Assignment of labile proton resonances in the heme cavity and determination of the distal glutamine orientation from relaxation data Journal of Biological Chemistry. 259: 8826-8831. PMID 6746625 |
0.423 |
|
| 1984 |
Jue T, La Mar GN. Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy. Biochemical and Biophysical Research Communications. 119: 640-5. PMID 6712648 DOI: 10.1016/S0006-291X(84)80297-1 |
0.598 |
|
| 1984 |
Krishnamoorthi R, La Mar GN, Mizukami H, Romero A. A proton NMR investigation of the influence of distal glutamine on structural and dynamic properties of elephant metmyoglobin Journal of Biological Chemistry. 259: 265-270. PMID 6706935 |
0.368 |
|
| 1984 |
La Mar GN, Jue T, Hoffman BM, Nagai K. Proton nuclear magnetic resonance investigation of the allosteric transition in ligated and unligated carp hemoglobin. Evidence for structural heterogeneity in the heme pocket. Journal of Molecular Biology. 178: 929-39. PMID 6492169 DOI: 10.1016/0022-2836(84)90320-6 |
0.636 |
|
| 1984 |
Jue T, La Mar GN, Han K, Yamamoto Y. NMR study of the exchange rates of allosterically responsive labile protons in the heme pockets of hemoglobin A. Biophysical Journal. 46: 117-20. PMID 6331541 DOI: 10.1016/S0006-3495(84)84004-7 |
0.618 |
|
| 1984 |
Lecomte J, La Mar GN, Winterhalter KH, Smit JDG. Proton nuclear magnetic resonance investigation of the heme cavity structure of liver fluke (Dirocoelium dendriticum) methemoglobin Journal of Molecular Biology. 180: 357-370. PMID 6096565 DOI: 10.1016/S0022-2836(84)80008-X |
0.343 |
|
| 1984 |
De Ropp JS, La Mar GN, Smith KM, Langry KC. Proton NMR studies of the electronic and molecular structure of ferric low-spin horseradish peroxidase complexes Journal of the American Chemical Society. 106: 4438-4444. |
0.325 |
|
| 1983 |
La Mar GN, Davis NL, Parish DW, Smith KM. Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the met-cyano protein Journal of Molecular Biology. 168: 887-896. PMID 6887254 DOI: 10.1016/S0022-2836(83)80080-1 |
0.336 |
|
| 1983 |
La Mar GN, Krishnamoorthi R. Proton magnetic resonance study of the influence of heme 2,4 substituents on the exchange rates of labile protons in the heme pocket of myoglobin Biophysical Journal. 44: 177-183. PMID 6317075 DOI: 10.1016/S0006-3495(83)84289-1 |
0.324 |
|
| 1983 |
Jue T, Krishnamoorthi R, La Mar GN. Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin Journal of the American Chemical Society. 105: 5701-5703. DOI: 10.1021/Ja00355A036 |
0.541 |
|
| 1983 |
La Mar GN, Krishnamoorthi R, Smith KM, Gersonde K, Sick H. Proton nuclear magnetic resonance investigation of the conformation-dependent spin equilibrium in azide-ligated monomeric insect hemoglobins Biochemistry. 22: 6239-6246. DOI: 10.1021/Bi00295A031 |
0.307 |
|
| 1982 |
La Mar GN, Kong SB, Smith KM, Langry KC. Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR. Biochemical and Biophysical Research Communications. 102: 142-8. PMID 7197933 DOI: 10.1016/0006-291X(81)91500-X |
0.411 |
|
| 1982 |
Nagai K, La Mar GN, Jue T, Bunn HF. Proton magnetic resonance investigation of the influence of quaternary structure on iron-histidine bonding in deoxyhemoglobins. Biochemistry. 21: 842-7. PMID 7074055 DOI: 10.1021/Bi00534A005 |
0.597 |
|
| 1982 |
La Mar GN, De Ropp JS, Chacko VP, Satterlee JD, Erman JE. Axial histidyl imidazole non-exchangeable proton resonances as indicators of imidazole hydrogen bonding in ferric cyanide complexes of heme peroxidases Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 708: 317-325. PMID 6293582 DOI: 10.1016/0167-4838(82)90443-5 |
0.401 |
|
| 1982 |
Cutnell JD, La Mar GN, Dallas JL, Hug P, Rink H, Rist G. High-field 1H NMR studies of synthetic analogs of somatostatin. Structural features involving aromatic residues in an active eight-membered ring analog. Biochimica Et Biophysica Acta. 700: 59-66. PMID 6120004 DOI: 10.1016/0167-4838(82)90292-8 |
0.341 |
|
| 1981 |
La Mar GN, Anderson RR, Budd DL, Smith KM, Langry KC, Gersonde K, Sick H. Proton nuclear magnetic resonance investigation of the nature of solution conformational equilibria of monomeric insect deoxyhemoglobins. Biochemistry. 20: 4429-36. PMID 7284332 DOI: 10.1021/Bi00518A030 |
0.337 |
|
| 1981 |
La Mar GN, Cutnell JD, Kong SB. Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole. Biophysical Journal. 34: 217-26. PMID 7236849 DOI: 10.1016/S0006-3495(81)84846-1 |
0.32 |
|
| 1980 |
La Mar GN, Nagai K, Jue T, Budd DL, Gersonde K, Sick H, Kagimoto T, Hayashi A, Taketa F. Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. Biochemical and Biophysical Research Communications. 96: 1172-7. PMID 7437062 DOI: 10.1016/0006-291X(80)90075-3 |
0.534 |
|
| 1979 |
La Mar GN, Budd DL. Proton NMR study of model substrate binding in hemoproteins. Intercalation of mercuric triiodide in sperm whale met-aquo myoglobin. Biochimica Et Biophysica Acta. 581: 201-9. PMID 518909 DOI: 10.1016/0005-2795(79)90239-3 |
0.339 |
|
| 1978 |
La Mar GN, Budd DL, Viscio DB, Smith KM, Langry KC. Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins. Proceedings of the National Academy of Sciences of the United States of America. 75: 5755-9. PMID 282600 DOI: 10.1073/Pnas.75.12.5755 |
0.373 |
|
| 1977 |
La Mar GN, Del Gaudio J, Frye JS. Axial pertubations on the electronic and magnetic properties of ferric porphyrins. II. Solvent effects on the proton NMR spectra of low-spin cyano complexes. Biochimica Et Biophysica Acta. 498: 422-35. PMID 884161 DOI: 10.1016/0304-4165(77)90280-X |
0.425 |
|
| 1977 |
La Mar GN, Bold TJ, Satterlee JD. Axial perturbations on the electronic and magnetic properties of ferric porphyrins I. Effect of axial ligand basicity in bis-substituted pyridine complexes of synthetic porphyrins Bba - General Subjects. 498: 189-207. PMID 884147 DOI: 10.1016/0304-4165(77)90099-X |
0.393 |
|
| 1977 |
La Mar GN, Budd DL, Goff H. Assignment of proximal histidine proton NMR peaks in myoglobin and hemoglobin. Biochemical and Biophysical Research Communications. 77: 104-10. PMID 883967 DOI: 10.1016/S0006-291X(77)80170-8 |
0.31 |
|
| 1977 |
Goff H, La Mar GN, Reed CA. Nuclear magnetic resonance investigation of magnetic and electronic properties of "intermediate spin" ferrous porphyrin complexes Journal of the American Chemical Society. 99: 3641-3646. PMID 858871 DOI: 10.1021/ja00453a022 |
0.352 |
|
| 1977 |
Goff H, La Mar GN. High-spin ferrous porphyrin complexes as models for deoxymyoglobin and -hemoglobin. A proton nuclear magnetic resonance study. Journal of the American Chemical Society. 99: 6599-6709. PMID 197140 DOI: 10.1021/ja00462a022 |
0.303 |
|
| 1976 |
La Mar GN, Frye JS, Satterlee JD. Proton NMR study of coordinated imidazoles in low-spin ferric heme complexes. Assignment of single proton histidine resonance in hemoproteins. Biochimica Et Biophysica Acta. 428: 78-89. PMID 1260027 DOI: 10.1016/0304-4165(76)90110-0 |
0.41 |
|
| 1976 |
FULTON GP, LA MAR GN. ChemInform Abstract: PROTON NMR STUDIES OF THE INTERACTION OF METALLOPORPHYRINS WITH Π ACCEPTORS AND DONORS. I. EFFECT OF Π-COMPLEX FORMATION ON THE ELECTRONIC STRUCTURE OF LOW-SPIN COBALT(II) Chemischer Informationsdienst. 7: no-no. DOI: 10.1002/chin.197627069 |
0.32 |
|
| 1975 |
La Mar GN, Walker FA. Proton nuclear magnetic resonance studies of high-spin manganese(III) complexes with synthetic porphyrins. Journal of the American Chemical Society. 97: 5103-7. PMID 1165359 DOI: 10.1021/ja00851a013 |
0.305 |
|
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