Year |
Citation |
Score |
2023 |
Warmack RA, Maggiolo AO, Orta A, Wenke BB, Howard JB, Rees DC. Structural consequences of turnover-induced homocitrate loss in nitrogenase. Nature Communications. 14: 1091. PMID 36841829 DOI: 10.1038/s41467-023-36636-4 |
0.57 |
|
2015 |
Spatzal T, Perez KA, Howard JB, Rees DC. Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. Elife. 4. PMID 26673079 DOI: 10.7554/Elife.11620 |
0.568 |
|
2015 |
Tezcan FA, Kaiser JT, Howard JB, Rees DC. Structural evidence for asymmetrical nucleotide interactions in nitrogenase. Journal of the American Chemical Society. 137: 146-9. PMID 25522159 DOI: 10.1021/Ja511945E |
0.747 |
|
2015 |
Spatzal T, Perez KA, Howard JB, Rees DC. Author response: Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor Elife. DOI: 10.7554/Elife.11620.023 |
0.542 |
|
2015 |
Glazer AN, Kechris K, Howard JB. Distribution and Ecological Niches of Nitrogenases Biological Nitrogen Fixation. 87-98. DOI: 10.1002/9781119053095.Ch8 |
0.461 |
|
2014 |
Spatzal T, Perez KA, Einsle O, Howard JB, Rees DC. Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science (New York, N.Y.). 345: 1620-3. PMID 25258081 DOI: 10.1126/Science.1256679 |
0.712 |
|
2014 |
Yang KY, Haynes CA, Spatzal T, Rees DC, Howard JB. Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH. Biochemistry. 53: 333-43. PMID 24392967 DOI: 10.1021/Bi4014769 |
0.672 |
|
2013 |
Howard JB, Kechris KJ, Rees DC, Glazer AN. Multiple amino acid sequence alignment nitrogenase component 1: insights into phylogenetics and structure-function relationships. Plos One. 8: e72751. PMID 24019874 DOI: 10.1371/Journal.Pone.0072751 |
0.684 |
|
2013 |
Zhang L, Kaiser JT, Meloni G, Yang KY, Spatzal T, Andrade SL, Einsle O, Howard JB, Rees DC. The sixteenth iron in the nitrogenase MoFe protein. Angewandte Chemie (International Ed. in English). 52: 10529-32. PMID 23963815 DOI: 10.1002/Anie.201303877 |
0.743 |
|
2010 |
MAGNUSON JK, PAUSTIAN TD, SHAH VK, DEAN DR, ROBERTS GP, REES DC, HOWARD JB. ChemInform Abstract: Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding. Cheminform. 28: no-no. DOI: 10.1002/CHIN.199750256 |
0.523 |
|
2006 |
Howard JB, Rees DC. How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation. Proceedings of the National Academy of Sciences of the United States of America. 103: 17088-93. PMID 17088547 DOI: 10.1073/Pnas.0603978103 |
0.62 |
|
2005 |
Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC. Nitrogenase complexes: multiple docking sites for a nucleotide switch protein. Science (New York, N.Y.). 309: 1377-80. PMID 16123301 DOI: 10.1126/Science.1115653 |
0.735 |
|
2005 |
Rees DC, Akif Tezcan F, Haynes CA, Walton MY, Andrade S, Einsle O, Howard JB. Structural basis of biological nitrogen fixation. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 363: 971-84; discussion 1. PMID 15901546 DOI: 10.1098/Rsta.2004.1539 |
0.711 |
|
2003 |
Rees DC, Howard JB. The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science (New York, N.Y.). 300: 929-31. PMID 12738849 DOI: 10.1126/Science.1083075 |
0.56 |
|
2002 |
Schmid B, Einsle O, Chiu HJ, Willing A, Yoshida M, Howard JB, Rees DC. Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure. Biochemistry. 41: 15557-65. PMID 12501184 DOI: 10.1021/Bi026642B |
0.718 |
|
2002 |
Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science (New York, N.Y.). 297: 1696-700. PMID 12215645 DOI: 10.1126/Science.1073877 |
0.743 |
|
2001 |
Chiu H, Peters JW, Lanzilotta WN, Ryle MJ, Seefeldt LC, Howard JB, Rees DC. MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein. Biochemistry. 40: 641-50. PMID 11170380 DOI: 10.1021/Bi001645E |
0.649 |
|
2000 |
Rees DC, Howard JB. Nitrogenase: standing at the crossroads. Current Opinion in Chemical Biology. 4: 559-66. PMID 11006545 DOI: 10.1016/S1367-5931(00)00132-0 |
0.513 |
|
1999 |
Rees DC, Howard JB. Structural bioenergetics and energy transduction mechanisms. Journal of Molecular Biology. 293: 343-50. PMID 10550213 DOI: 10.1006/Jmbi.1999.3005 |
0.522 |
|
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 |
0.37 |
|
1999 |
Grossmann JG, Hasnain SS, Yousafzai FK, Smith BE, Eady RR, Schindelin H, Kisker C, Howard JB, Tsuruta H, Muller J, Rees DC. Comparing crystallographic and solution structures of nitrogenase complexes Acta Crystallographica Section D: Biological Crystallography. 55: 727-728. PMID 10336305 DOI: 10.1107/S0907444999003856 |
0.663 |
|
1998 |
Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC. Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. Journal of Molecular Biology. 280: 669-85. PMID 9677296 DOI: 10.1006/Jmbi.1998.1898 |
0.759 |
|
1997 |
Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC. Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature. 387: 370-6. PMID 9163420 DOI: 10.1038/387370A0 |
0.71 |
|
1997 |
Magnuson JK, Paustian TD, Shah VK, Dean DR, Roberts GP, Rees DC, Howard JB. Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding Tetrahedron. 53: 11971-11984. DOI: 10.1016/S0040-4020(97)00710-2 |
0.602 |
|
1996 |
Howard JB, Rees DC. Structural Basis of Biological Nitrogen Fixation. Chemical Reviews. 96: 2965-2982. PMID 11848848 DOI: 10.1021/Cr9500545 |
0.5 |
|
1996 |
Renner KA, Howard JB. Aluminum fluoride inhibition of nitrogenase: stabilization of a nucleotide.Fe-protein.MoFe-protein complex. Biochemistry. 35: 5353-8. PMID 8611524 DOI: 10.1021/Bi960441O |
0.484 |
|
1995 |
Gorst CM, Zhou ZH, Ma K, Teng Q, Howard JB, Adams MW, La Mar GN. Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature. Biochemistry. 34: 8788-95. PMID 7612619 DOI: 10.1021/Bi00027A030 |
0.38 |
|
1994 |
Eccleston ED, White TW, Howard JB, Hamilton DW. Characterization of a cell surface glycoprotein associated with maturation of rat spermatozoa. Molecular Reproduction and Development. 37: 110-9. PMID 8129926 DOI: 10.1002/Mrd.1080370115 |
0.395 |
|
1994 |
Howard JB, Rees DC. Nitrogenase: a nucleotide-dependent molecular switch. Annual Review of Biochemistry. 63: 235-64. PMID 7979238 DOI: 10.1146/Annurev.Bi.63.070194.001315 |
0.516 |
|
1992 |
Wolle D, Kim C, Dean D, Howard JB. Ionic interactions in the nitrogenase complex. Properties of Fe-protein containing substitutions for Arg-100. The Journal of Biological Chemistry. 267: 3667-73. PMID 1740419 |
0.379 |
|
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 |
0.377 |
|
1992 |
Wolle D, Dean DR, Howard JB. Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125. Science (New York, N.Y.). 258: 992-5. PMID 1359643 DOI: 10.1126/Science.1359643 |
0.495 |
|
1991 |
Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard JB, Summers MF, Adams MW. Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR. Biochemistry. 30: 10885-95. PMID 1932012 DOI: 10.1021/Bi00109A012 |
0.438 |
|
1991 |
Howard JB, Rees DC. Perspectives on non-heme iron protein chemistry. Advances in Protein Chemistry. 42: 199-280. PMID 1793006 DOI: 10.1016/S0065-3233(08)60537-9 |
0.616 |
|
1990 |
Willing A, Howard JB. Cross-linking site in Azotobacter vinelandii complex. The Journal of Biological Chemistry. 265: 6596-9. PMID 2324093 |
0.407 |
|
1989 |
McFarlan SC, Hogenkamp HP, Eccleston ED, Howard JB, Fuchs JA. Purification, characterization and revised amino acid sequence of a second thioredoxin from Corynebacterium nephridii. European Journal of Biochemistry / Febs. 179: 389-98. PMID 2917572 DOI: 10.1111/J.1432-1033.1989.Tb14565.X |
0.32 |
|
1989 |
Deits TL, Howard JB. Kinetics of MgATP-dependent iron chelation from the Fe-protein of the Azotobacter vinelandii nitrogenase complex. Evidence for two states. The Journal of Biological Chemistry. 264: 6619-28. PMID 2785107 |
0.313 |
|
1989 |
Willing AH, Georgiadis MM, Rees DC, Howard JB. Cross-linking of nitrogenase components. Structure and activity of the covalent complex. The Journal of Biological Chemistry. 264: 8499-503. PMID 2722786 |
0.531 |
|
1989 |
Adams MW, Eccleston E, Howard JB. Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum. Proceedings of the National Academy of Sciences of the United States of America. 86: 4932-6. PMID 2544883 DOI: 10.1073/Pnas.86.13.4932 |
0.376 |
|
1989 |
Howard JB, Davis R, Moldenhauer B, Cash VL, Dean D. Fe:S cluster ligands are the only cysteines required for nitrogenase Fe-protein activities. The Journal of Biological Chemistry. 264: 11270-4. PMID 2500438 |
0.363 |
|
1984 |
Anderson GL, Howard JB. Reactions with the oxidized iron protein of Azotobacter vinelandii nitrogenase: formation of a 2Fe center. Biochemistry. 23: 2118-22. PMID 6329264 DOI: 10.1021/Bi00305A002 |
0.414 |
|
1983 |
Hausinger RP, Howard JB. Thiol reactivity of the nitrogenase Fe-protein from Azotobacter vinelandii. The Journal of Biological Chemistry. 258: 13486-92. PMID 6580291 |
0.617 |
|
1983 |
Rees DC, Howard JB. Crystallization of the Azotobacter vinelandii nitrogenase iron protein. The Journal of Biological Chemistry. 258: 12733-4. PMID 6579051 |
0.523 |
|
1983 |
Howard JB, Swenson R, Eccleston E. The methylamine reactive site and protease inhibition in alpha 2-macroglobulin. Annals of the New York Academy of Sciences. 421: 160-6. PMID 6202192 DOI: 10.1111/J.1749-6632.1983.Tb18106.X |
0.629 |
|
1982 |
Hausinger RP, Howard JB. The amino acid sequence of the nitrogenase iron protein from Azotobacter vinelandii. The Journal of Biological Chemistry. 257: 2483-90. PMID 6801032 |
0.568 |
|
1982 |
Hausinger RP, Moura I, Moura JJ, Xavier AV, Santos MH, LeGall J, Howard JB. Amino acid sequence of a 3Fe:3S ferredoxin from the "archaebacterium" Methanosarcina barkeri (DSM 800). The Journal of Biological Chemistry. 257: 14192-7. PMID 6754724 |
0.572 |
|
1980 |
Hausinger RP, Howard JB. Comparison of the iron proteins from the nitrogen fixation complexes of Azotobacter vinelandii, Clostridium pasteurianum, and Klebsiella pneumoniae. Proceedings of the National Academy of Sciences of the United States of America. 77: 3826-30. PMID 7001444 DOI: 10.1073/Pnas.77.7.3826 |
0.641 |
|
1980 |
Swenson RP, Howard JB. Amino acid sequence of the tryptic peptide containing the alkylamine-reactive site from human alpha 2-macroglobulin. Identification of gamma-glutamylmethylamide. The Journal of Biological Chemistry. 255: 8087-91. PMID 6157682 |
0.632 |
|
1980 |
Howard JB, Vermeulen M, Swenson RP. The temperature-sensitive bond in human alpha 2-macroglobulin is the alkylamine-reactive site. The Journal of Biological Chemistry. 255: 3820-3. PMID 6154704 |
0.588 |
|
1979 |
Swenson RP, Howard JB. Characterization of alkylamine-sensitive site in alpha 2-macroglobulin. Proceedings of the National Academy of Sciences of the United States of America. 76: 4313-6. PMID 92026 DOI: 10.1073/Pnas.76.9.4313 |
0.67 |
|
1979 |
Swenson RP, Howard JB. Structural characterization of human alpha2-macroglobulin subunits. The Journal of Biological Chemistry. 254: 4452-6. PMID 86541 |
0.607 |
|
1978 |
Lundell DJ, Howard JB. Isolation and partial characterization of two different subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase. The Journal of Biological Chemistry. 253: 3422-6. PMID 649581 |
0.305 |
|
1976 |
Howard JB, Lorsbach T, Que L. Iron-sulfur clusters and cysteine distribution in a ferredoxin from Azotobacter vinelandii. Biochemical and Biophysical Research Communications. 70: 582-8. PMID 938514 DOI: 10.1016/0006-291X(76)91087-1 |
0.328 |
|
1975 |
Nelsestuen GL, Broderius M, Zytkovicz TH, Howard JB. On the role of gamma-carboxyglutamic acid in calcium and phospholipid binding. Biochemical and Biophysical Research Communications. 65: 233-40. PMID 1147986 DOI: 10.1016/S0006-291X(75)80084-2 |
0.305 |
|
1969 |
Glazer AN, Barel AO, Howard JB, Brown DM. Isolation and characterization of fig lysozyme. The Journal of Biological Chemistry. 244: 3583-9. PMID 5794227 |
0.428 |
|
1969 |
Howard JB, Glazer AN. Papaya lysozyme. Terminal sequences and enzymatic properties. The Journal of Biological Chemistry. 244: 1399-409. PMID 5773045 |
0.457 |
|
1967 |
Howard JB, Glazer AN. Studies of the physicochemical and enzymatic properties of papaya lysozyme. The Journal of Biological Chemistry. 242: 5715-23. PMID 5633400 |
0.433 |
|
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