| Year |
Citation |
Score |
| 2020 |
Geeraerts Z, Heskin AK, DuBois J, Rodgers KR, Lukat-Rodgers GS. Structure and reactivity of chlorite dismutase nitrosyls. Journal of Inorganic Biochemistry. 211: 111203. PMID 32768737 DOI: 10.1016/J.Jinorgbio.2020.111203 |
0.422 |
|
| 2018 |
Linder DP, Baker BE, Rodgers KR. [(HO)Zn(Imidazole)]: the vital roles of coordination number and geometry in Zn-OH acidity and catalytic hydrolysis. Physical Chemistry Chemical Physics : Pccp. PMID 30239541 DOI: 10.1039/C8Cp03121E |
0.341 |
|
| 2018 |
McWilliams SF, Bill E, Lukat-Rodgers G, Rodgers KR, Mercado BQ, Holland PL. Effects of N Binding Mode on Iron-Based Functionalization of Dinitrogen to Form an Iron(III) Hydrazido Complex. Journal of the American Chemical Society. PMID 29957940 DOI: 10.1021/Jacs.8B04828 |
0.381 |
|
| 2018 |
Streit BR, Celis AI, Moraski GC, Shisler K, Shepard EM, Rodgers KR, Lukat-Rodgers GS, DuBois JL. Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b. The Journal of Biological Chemistry. PMID 29414780 DOI: 10.1074/Jbc.Ra117.000830 |
0.411 |
|
| 2018 |
Geeraerts Z, Celis AI, Mayfield JA, Lorenz M, Rodgers KR, DuBois JL, Lukat-Rodgers GS. Distinguishing active site characteristics of chlorite dismutases with their cyanide complexes. Biochemistry. PMID 29406727 DOI: 10.1021/Acs.Biochem.7B01278 |
0.429 |
|
| 2017 |
Geeraerts Z, Rodgers KR, DuBois J, Lukat-Rodgers GS. Active sites of O2-evolving chlorite dismutases probed by halides, hydroxides and new iron-ligand vibrational correlations. Biochemistry. PMID 28758386 DOI: 10.1021/Acs.Biochem.7B00572 |
0.437 |
|
| 2017 |
DeRosha DE, Mercado BQ, Lukat-Rodgers G, Rodgers KR, Holland PL. Enhancement of C-H Oxidizing Ability in Co-O2 Complexes through an Isolated Heterobimetallic Oxo Intermediate. Angewandte Chemie (International Ed. in English). 56: 3211-3215. PMID 28194845 DOI: 10.1002/Anie.201612010 |
0.385 |
|
| 2016 |
Streit BR, Celis AI, Shisler K, Rodgers KR, Lukat-Rodgers GS, DuBois JL. Reactions of Ferrous Coproheme Decarboxylase (HemQ) with O2 and H2O2 Yield Ferric Heme b. Biochemistry. PMID 27982566 DOI: 10.1021/Acs.Biochem.6B00958 |
0.419 |
|
| 2016 |
Uluisik RC, Akbas N, Lukat-Rodgers GS, Adrian SA, Allen CE, Schmitt MP, Rodgers KR, Dixon DW. Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae. Journal of Inorganic Biochemistry. 167: 124-133. PMID 27974280 DOI: 10.1016/J.Jinorgbio.2016.11.027 |
0.371 |
|
| 2016 |
Celis AI, Gauss GH, Streit BR, Shisler K, Moraski GC, Rodgers KR, Lukat-Rodgers GS, Peters JW, DuBois JL. A Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ). Journal of the American Chemical Society. PMID 27936663 DOI: 10.1021/Jacs.6B11324 |
0.39 |
|
| 2016 |
Hines JP, Smith AT, Jacob JP, Lukat-Rodgers GS, Barr I, Rodgers KR, Guo F, Burstyn JN. CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27766492 DOI: 10.1007/S00775-016-1398-Z |
0.362 |
|
| 2016 |
Draganova EB, Adrian SA, Lukat-Rodgers GS, Keutcha CS, Schmitt MP, Rodgers KR, Dixon DW. Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27561288 DOI: 10.1007/S00775-016-1386-3 |
0.41 |
|
| 2016 |
McWilliams SF, Rodgers KR, Lukat-Rodgers G, Mercado BQ, Grubel K, Holland PL. Alkali Metal Variation and Twisting of the FeNNFe Core in Bridging Diiron Dinitrogen Complexes. Inorganic Chemistry. 55: 2960-8. PMID 26925968 DOI: 10.1021/Acs.Inorgchem.5B02841 |
0.323 |
|
| 2015 |
Akbas N, Draganova EB, Block DR, Sook BR, Chan YF, Zhuo J, Eichenbaum Z, Rodgers KR, Dixon DW. Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability. Journal of Inorganic Biochemistry. PMID 26746808 DOI: 10.1016/J.Jinorgbio.2015.10.016 |
0.708 |
|
| 2015 |
Draganova EB, Akbas N, Adrian SA, Lukat-Rodgers GS, Collins DP, Dawson JH, Allen CE, Schmitt MP, Rodgers KR, Dixon DW. Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment. Biochemistry. 54: 6598-609. PMID 26478504 DOI: 10.1021/Acs.Biochem.5B00666 |
0.459 |
|
| 2015 |
Celis AI, Streit BR, Moraski GC, Kant R, Lash TD, Lukat-Rodgers GS, Rodgers KR, DuBois JL. Unusual Peroxide-Dependent, Heme-Transforming Reaction Catalyzed by HemQ. Biochemistry. PMID 26083961 DOI: 10.1021/Acs.Biochem.5B00492 |
0.361 |
|
| 2014 |
Babbitt SE, San Francisco B, Mendez DL, Lukat-Rodgers GS, Rodgers KR, Bretsnyder EC, Kranz RG. Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His. The Journal of Biological Chemistry. 289: 28795-807. PMID 25170082 DOI: 10.1074/Jbc.M114.593509 |
0.356 |
|
| 2014 |
Mokry DZ, Nadia-Albete A, Johnson MK, Lukat-Rodgers GS, Rodgers KR, Lanzilotta WN. Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor. Biochimica Et Biophysica Acta. 1840: 3058-66. PMID 24968987 DOI: 10.1016/J.Bbagen.2014.06.009 |
0.36 |
|
| 2014 |
Linder DP, Silvernail NJ, Barabanschikov A, Zhao J, Alp EE, Sturhahn W, Sage JT, Scheidt WR, Rodgers KR. The diagnostic vibrational signature of pentacoordination in heme carbonyls. Journal of the American Chemical Society. 136: 9818-21. PMID 24950373 DOI: 10.1021/Ja503191Z |
0.403 |
|
| 2013 |
Mayfield JA, Blanc B, Rodgers KR, Lukat-Rodgers GS, DuBois JL. Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase. Biochemistry. 52: 6982-94. PMID 24001266 DOI: 10.1021/Bi4005599 |
0.3 |
|
| 2013 |
Blanc B, Rodgers KR, Lukat-Rodgers GS, DuBois JL. Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases. Dalton Transactions (Cambridge, England : 2003). 42: 3156-69. PMID 23241559 DOI: 10.1039/C2Dt32312E |
0.427 |
|
| 2012 |
Caillet-Saguy C, Piccioli M, Turano P, Lukat-Rodgers G, Wolff N, Rodgers KR, Izadi-Pruneyre N, Delepierre M, Lecroisey A. Role of the iron axial ligands of heme carrier HasA in heme uptake and release. The Journal of Biological Chemistry. 287: 26932-43. PMID 22700962 DOI: 10.1074/Jbc.M112.366385 |
0.404 |
|
| 2012 |
Blanc B, Mayfield JA, McDonald CA, Lukat-Rodgers GS, Rodgers KR, DuBois JL. Understanding how the distal environment directs reactivity in chlorite dismutase: spectroscopy and reactivity of Arg183 mutants. Biochemistry. 51: 1895-910. PMID 22313119 DOI: 10.1021/Bi2017377 |
0.42 |
|
| 2011 |
San Francisco B, Bretsnyder EC, Rodgers KR, Kranz RG. Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF. Biochemistry. 50: 10974-85. PMID 22066495 DOI: 10.1021/Bi201508T |
0.401 |
|
| 2011 |
Ostera G, Tokumasu F, Teixeira C, Collin N, Sa J, Hume J, Kumar S, Ribeiro J, Lukat-Rodgers GS, Rodgers KR. Plasmodium falciparum: nitric oxide modulates heme speciation in isolated food vacuoles. Experimental Parasitology. 127: 1-8. PMID 20493843 DOI: 10.1016/J.Exppara.2010.05.006 |
0.349 |
|
| 2010 |
Lukat-Rodgers GS, Correia C, Botuyan MV, Mer G, Rodgers KR. Heme-based sensing by the mammalian circadian protein CLOCK. Inorganic Chemistry. 49: 6349-65. PMID 20666392 DOI: 10.1021/Ic902388Q |
0.416 |
|
| 2010 |
Streit BR, Blanc B, Lukat-Rodgers GS, Rodgers KR, DuBois JL. How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase. Journal of the American Chemical Society. 132: 5711-24. PMID 20356038 DOI: 10.1021/Ja9082182 |
0.46 |
|
| 2009 |
Reynolds MF, Ackley L, Blizman A, Lutz Z, Manoff D, Miles M, Pace M, Patterson J, Pozzessere N, Saia K, Sato R, Smith D, Tarves P, Weaver M, Sieg K, ... ... Rodgers KR, et al. Role of conserved F(alpha)-helix residues in the native fold and stability of the kinase-inhibited oxy state of the oxygen-sensing FixL protein from Sinorhizobium meliloti. Archives of Biochemistry and Biophysics. 485: 150-9. PMID 19254684 DOI: 10.1016/J.Abb.2009.02.011 |
0.32 |
|
| 2008 |
Sook BR, Block DR, Sumithran S, Montañez GE, Rodgers KR, Dawson JH, Eichenbaum Z, Dixon DW. Characterization of SiaA, a streptococcal heme-binding protein associated with a heme ABC transport system. Biochemistry. 47: 2678-88. PMID 18247478 DOI: 10.1021/Bi701604Y |
0.717 |
|
| 2008 |
Lukat-Rodgers GS, Rodgers KR, Caillet-Saguy C, Izadi-Pruneyre N, Lecroisey A. Novel heme ligand displacement by CO in the soluble hemophore HasA and its proximal ligand mutants: implications for heme uptake and release. Biochemistry. 47: 2087-98. PMID 18205408 DOI: 10.1021/Bi7019518 |
0.475 |
|
| 2008 |
Caillet-Saguy C, Turano P, Piccioli M, Lukat-Rodgers GS, Czjzek M, Guigliarelli B, Izadi-Pruneyre N, Rodgers KR, Delepierre M, Lecroisey A. Deciphering the structural role of histidine 83 for heme binding in hemophore HasA. The Journal of Biological Chemistry. 283: 5960-70. PMID 18162469 DOI: 10.1074/Jbc.M703795200 |
0.396 |
|
| 2007 |
Block DR, Lukat-Rodgers GS, Rodgers KR, Wilks A, Bhakta MN, Lansky IB. Identification of two heme-binding sites in the cytoplasmic heme-trafficking protein PhuS from Pseudomonas aeruginosa and their relevance to function. Biochemistry. 46: 14391-402. PMID 18020455 DOI: 10.1021/Bi701509N |
0.715 |
|
| 2007 |
Linder DP, Rodgers KR. Computational modeling of factors that modulate the unique FeNO bonding in {FeNO}(6) heme-thiolate model complexes. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 721-31. PMID 17356871 DOI: 10.1007/S00775-007-0223-0 |
0.356 |
|
| 2006 |
Cowley AB, Kennedy ML, Silchenko S, Lukat-Rodgers GS, Rodgers KR, Benson DR. Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptides. Inorganic Chemistry. 45: 9985-10001. PMID 17140194 DOI: 10.1021/Ic052205K |
0.396 |
|
| 2006 |
Izadi-Pruneyre N, Huché F, Lukat-Rodgers GS, Lecroisey A, Gilli R, Rodgers KR, Wandersman C, Delepelaire P. The heme transfer from the soluble HasA hemophore to its membrane-bound receptor HasR is driven by protein-protein interaction from a high to a lower affinity binding site. The Journal of Biological Chemistry. 281: 25541-50. PMID 16774915 DOI: 10.1074/Jbc.M603698200 |
0.422 |
|
| 2006 |
Lansky IB, Lukat-Rodgers GS, Block D, Rodgers KR, Ratliff M, Wilks A. The cytoplasmic heme-binding protein (PhuS) from the heme uptake system of Pseudomonas aeruginosa is an intracellular heme-trafficking protein to the delta-regioselective heme oxygenase. The Journal of Biological Chemistry. 281: 13652-62. PMID 16533806 DOI: 10.1074/Jbc.M600824200 |
0.737 |
|
| 2005 |
Pazicni S, Cherney MM, Lukat-Rodgers GS, Oliveriusová J, Rodgers KR, Kraus JP, Burstyn JN. The heme of cystathionine beta-synthase likely undergoes a thermally induced redox-mediated ligand switch. Biochemistry. 44: 16785-95. PMID 16363792 DOI: 10.1021/Bi051305Z |
0.43 |
|
| 2005 |
He H, Puerta DT, Cohen SM, Rodgers KR. Structural and spectroscopic study of reactions between chelating zinc-binding groups and mimics of the matrix metalloproteinase and disintegrin metalloprotease catalytic sites: the coordination chemistry of metalloprotease inhibition. Inorganic Chemistry. 44: 7431-42. PMID 16212369 DOI: 10.1021/Ic050723P |
0.405 |
|
| 2005 |
Eakanunkul S, Lukat-Rodgers GS, Sumithran S, Ghosh A, Rodgers KR, Dawson JH, Wilks A. Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae. Biochemistry. 44: 13179-91. PMID 16185086 DOI: 10.1021/Bi050422R |
0.361 |
|
| 2005 |
Rodgers KR, Lukat-Rodgers GS. Insights into heme-based O2 sensing from structure-function relationships in the FixL proteins. Journal of Inorganic Biochemistry. 99: 963-77. PMID 15811514 DOI: 10.1016/J.Jinorgbio.2005.02.016 |
0.432 |
|
| 2005 |
Linder DP, Rodgers KR. Fe-N-O structure and bonding in six-coordinate {FeNO}6 porphyrinates containing imidazole: implications for reactivity of coordinated NO. Inorganic Chemistry. 44: 1367-80. PMID 15732977 DOI: 10.1021/Ic049045H |
0.364 |
|
| 2004 |
Pazicni S, Lukat-Rodgers GS, Oliveriusová J, Rees KA, Parks RB, Clark RW, Rodgers KR, Kraus JP, Burstyn JN. The redox behavior of the heme in cystathionine beta-synthase is sensitive to pH. Biochemistry. 43: 14684-95. PMID 15544339 DOI: 10.1021/Bi0488496 |
0.361 |
|
| 2004 |
Linder DP, Rodgers KR, Banister J, Wyllie GR, Ellison MK, Scheidt WR. Five-coordinate Fe(III)NO and Fe(II)CO porphyrinates: where are the electrons and why does it matter? Journal of the American Chemical Society. 126: 14136-48. PMID 15506779 DOI: 10.1021/Ja046942B |
0.388 |
|
| 2004 |
He H, Rodgers KR, Arif AM. Structural and spectroscopic studies of tripodal [MgL]2+ chelates containing only nitrogen donor atoms: alkaline earth metal complexes as potential drug delivery agents. Journal of Inorganic Biochemistry. 98: 667-76. PMID 15134911 DOI: 10.1016/J.Jinorgbio.2004.02.018 |
0.362 |
|
| 2004 |
Cowley AB, Lukat-Rodgers GS, Rodgers KR, Benson DR. A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide. Biochemistry. 43: 1656-66. PMID 14769043 DOI: 10.1021/Bi035531P |
0.436 |
|
| 2004 |
Linder DP, Rodgers KR. A theoretical study of imidazole- and thiol-based zinc binding groups relevant to inhibition of metzincins Journal of Physical Chemistry B. 108: 13839-13849. DOI: 10.1021/Jp037474F |
0.343 |
|
| 2003 |
Lushington GH, Cowley AB, Silchenko S, Lukat-Rodgers GS, Rodgers KR, Benson DR. Comparison of thioethers and sulfoxides as axial ligands for N-acetylmicroperoxidase-8: implications for oxidation of methionine-80 in cytochrome c. Inorganic Chemistry. 42: 7550-9. PMID 14606851 DOI: 10.1021/Ic034689V |
0.443 |
|
| 2003 |
Andrew CR, Rodgers KR, Eady RR. A novel kinetic trap for NO release from cytochrome c': a possible mechanism for NO release from activated soluble guanylate cyclase. Journal of the American Chemical Society. 125: 9548-9. PMID 12903995 DOI: 10.1021/Ja035105R |
0.418 |
|
| 2002 |
Smith K, Silvernail NJ, Rodgers KR, Elgren TE, Castro M, Parker RM. Sol-gel encapsulated horseradish peroxidase: a catalytic material for peroxidation. Journal of the American Chemical Society. 124: 4247-52. PMID 11960453 DOI: 10.1021/Ja012215U |
0.356 |
|
| 2001 |
Rodgers KR, Tang L, Lukat-Rodgers GS, Wengenack NL. Insights into the signal transduction mechanism of RmFixL provided by carbon monoxide recombination kinetics. Biochemistry. 40: 12932-42. PMID 11669630 DOI: 10.1021/Bi011237Q |
0.355 |
|
| 2001 |
Fazal MA, Roy BC, Sun S, Mallik S, Rodgers KR. Surface recognition of a protein using designed transition metal complexes. Journal of the American Chemical Society. 123: 6283-90. PMID 11427052 DOI: 10.1021/Ja003193Z |
0.341 |
|
| 2001 |
Lukat-Rodgers GS, Wengenack NL, Rusnak F, Rodgers KR. Carbon monoxide adducts of KatG and KatG(S315T) as probes of the heme site and isoniazid binding. Biochemistry. 40: 7149-57. PMID 11401561 DOI: 10.1021/Bi010369G |
0.438 |
|
| 2001 |
Rodgers KR, Lukat-Rodgers GS, Tang L. Nitrosyl adducts of FixL as probes of heme environment. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 642-54. PMID 11085655 DOI: 10.1007/S007750000150 |
0.354 |
|
| 2000 |
Lukat-Rodgers GS, Wengenack NL, Rusnak F, Rodgers KR. Spectroscopic comparison of the heme active sites in WT KatG and its S315T mutant. Biochemistry. 39: 9984-93. PMID 10933819 DOI: 10.1021/Bi0006870 |
0.4 |
|
| 2000 |
Holland PL, Cramer CJ, Wilkinson EC, Mahapatra S, Rodgers KR, Itoh S, Taki M, Fukuzumi S, Que L, Tolman WB. Resonance Raman spectroscopy as a probe of the bis(μ-oxo)dicopper core Journal of the American Chemical Society. 122: 792-802. DOI: 10.1021/Ja992003L |
0.367 |
|
| 1999 |
Holland PL, Rodgers KR, Tolman WB. Is the Bis(μ-oxo)dicopper Core Capable of Hydroxylating an Arene? Angewandte Chemie (International Ed. in English). 38: 1139-42. PMID 25138522 DOI: 10.1002/(Sici)1521-3773(19990419)38:8<1139::Aid-Anie1139>3.0.Co;2-0 |
0.335 |
|
| 1999 |
Rodgers KR. Heme-based sensors in biological systems. Current Opinion in Chemical Biology. 3: 158-67. PMID 10226051 DOI: 10.1016/S1367-5931(99)80028-3 |
0.318 |
|
| 1999 |
Hu X, Rodgers KR, Mukerji I, Spiro TG. New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin kempsey. Biochemistry. 38: 3462-7. PMID 10090732 DOI: 10.1021/Bi982513C |
0.483 |
|
| 1998 |
Gerasimchuk NN, Mokhir AA, Rodgers KR. Synthesis and Characterization of Dimeric Mutually Coordinated Magnesium meso-2-Pyridylporphyrins. Inorganic Chemistry. 37: 5641-5650. PMID 11670713 DOI: 10.1021/Ic971421T |
0.357 |
|
| 1998 |
Lukat-Rodgers GS, Rexine JL, Rodgers KR. Heme speciation in alkaline ferric FixL and possible tyrosine involvement in the signal transduction pathway for regulation of nitrogen fixation. Biochemistry. 37: 13543-52. PMID 9753440 DOI: 10.1021/Bi981439V |
0.425 |
|
| 1998 |
Lukat-Rodgers GS, Rodgers KR. Spin-state equilibria and axial ligand bonding in FixL hydroxide: a resonance raman study Jbic Journal of Biological Inorganic Chemistry. 3: 274-281. DOI: 10.1007/S007750050232 |
0.43 |
|
| 1998 |
Smulevich G, Hu S, Rodgers KR, Goodin DB, Smith KM, Spiro TG. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes Biospectroscopy. 2: 365-376. DOI: 10.1002/(SICI)1520-6343(1996)2:6<365::AID-BSPY3>3.0.CO;2-2 |
0.466 |
|
| 1997 |
Lukat-Rodgers GS, Rodgers KR. Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy. Biochemistry. 36: 4178-87. PMID 9100012 DOI: 10.1021/Bi9628230 |
0.393 |
|
| 1997 |
Jayaraman V, Rodgers K, Mukerji I, Hu X, Spiro T. Metal coordination and protein dynamics: The allosteric reaction coordinate in hemoglobin Journal of Inorganic Biochemistry. 67: 79. DOI: 10.1016/S0162-0134(97)89959-X |
0.464 |
|
| 1996 |
Rodgers KR, Lukat-Rodgers GS, Barron JA. Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL. Biochemistry. 35: 9539-48. PMID 8755735 DOI: 10.1021/Bi9530853 |
0.46 |
|
| 1996 |
Smulevich G, Hu S, Rodgers KR, Goodin DB, Smith KM, Spiro TG. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance raman spectra of isotopically labeled hemes Biospectroscopy. 2: 365-376. DOI: 10.1002/(Sici)1520-6343(1996)2:6<365::Aid-Bspy3>3.0.Co;2-2 |
0.529 |
|
| 1995 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science (New York, N.Y.). 269: 1843-8. PMID 7569921 DOI: 10.1126/Science.7569921 |
0.612 |
|
| 1995 |
Bakac A, Scott SL, Espenson JH, Rodgers KR. Interaction of chromium(II) complexes with molecular oxygen. Spectroscopic and kinetic evidence for η1-superoxo complex formation Journal of the American Chemical Society. 117: 6483-6488. DOI: 10.1021/Ja00129A010 |
0.335 |
|
| 1994 |
Austin JC, Rodgers KR, Spiro TG. Protein structure from ultraviolet resonance Raman spectroscopy. Methods in Enzymology. 226: 374-96. PMID 8277873 DOI: 10.1016/0076-6879(93)26017-4 |
0.521 |
|
| 1994 |
Rodgers KR, Spiro TG. Nanosecond dynamics of the R-->T transition in hemoglobin: ultraviolet Raman studies. Science (New York, N.Y.). 265: 1697-9. PMID 8085153 DOI: 10.1126/Science.8085153 |
0.491 |
|
| 1993 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. R and T states of fluoromethemoglobin probed by ultraviolet resonance Raman spectroscopy. Biochemistry. 32: 4547-51. PMID 8485131 DOI: 10.1021/Bi00068A009 |
0.584 |
|
| 1993 |
Rodgers K, Mukerji I, Jayaraman V, Spiro T. Hemoglobin dynamics from transient raman spectroscopy Journal of Inorganic Biochemistry. 51: 215. DOI: 10.1016/0162-0134(93)85249-8 |
0.574 |
|
| 1992 |
Rodgers KR, Su C, Subramaniam S, Spiro TG. Hemoglobin R.fwdarw.T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals Journal of the American Chemical Society. 114: 3697-3709. DOI: 10.1021/Ja00036A019 |
0.48 |
|
| 1992 |
Rodgers KR, Reed RA, Su YO, Spiro TG. Resonance Raman and magnetic resonance spectroscopic characterization of the Fe(I), Fe(II), Fe(III), and Fe(IV) oxidation states of Fe(2-TMPyP)n+(aq) Inorganic Chemistry. 31: 2688-2700. DOI: 10.1021/Ic00039A007 |
0.535 |
|
| 1990 |
Reed RA, Rodgers KR, Kushmeider K, Spiro TG, Su YO. Iron-hydroxide stretching resonance Raman bands of a water-soluble sterically hindered porphyrin Inorganic Chemistry. 29: 2881-2883. DOI: 10.1021/Ic00341A003 |
0.563 |
|
| 1989 |
Lukat GS, Rodgers KR, Jabro MN, Goff HM. Magnetic resonance spectral characterization of the heme active site of Coprinus cinereus peroxidase. Biochemistry. 28: 3338-45. PMID 2545257 DOI: 10.1021/Bi00434A032 |
0.675 |
|
| 1988 |
Lukat GS, Jabro MN, Rodgers KR, Goff HM. Electron paramagnetic resonance spectroscopy of thyroid peroxidase. Biochimica Et Biophysica Acta. 954: 265-70. PMID 2835983 DOI: 10.1016/0167-4838(88)90081-7 |
0.571 |
|
| 1988 |
Lukat GS, Rodgers KR, Goff HM. Electron paramagnetic resonance spectroscopy of lactoperoxidase complexes: clarification of hyperfine splitting for the NO adduct of lactoperoxidase. Biochemistry. 26: 6927-32. PMID 2827739 DOI: 10.1021/Bi00396A011 |
0.675 |
|
| 1988 |
Rodgers KR, Goff HM. Generation and characterization of highly reactive oxo-transfer intermediates and related species derived from (tetraarylporphinato)manganese(III) complexes Journal of the American Chemical Society. 110: 7049-7060. DOI: 10.1021/Ja00229A018 |
0.581 |
|
| 1987 |
Rodgers KR, Goff HM. Detection of high-valent intermediates in the chlorine(I) oxidation of (porphinato)manganese(III) complexes Journal of the American Chemical Society. 109: 611-612. DOI: 10.1021/Ja00236A065 |
0.601 |
|
| 1985 |
Rodgers KR, Murmann RK, Schlemper EO, Shelton ME. Rates of isotopic oxygen exchange with solvent and oxygen atom transfer involving nonaaquatetraoxotrimolybdenum(4+) ([Mo3O4(OH2)9]4+) Inorganic Chemistry. 24: 1313-1322. DOI: 10.1021/Ic00203A011 |
0.658 |
|
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