Year |
Citation |
Score |
2023 |
Dobrzyńska K, Pérez-González A, Echavarri-Erasun C, Coroian D, Salinero-Lanzarote A, Veldhuizen M, Dean DR, Burén S, Rubio LM. Nitrogenase cofactor biosynthesis using proteins produced in mitochondria of . Mbio. e0308823. PMID 38126768 DOI: 10.1128/mbio.03088-23 |
0.301 |
|
2023 |
Dean DR, Martin Del Campo JS. Trp-ing out on cytosolic [Fe-S]-cluster delivery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2317221120. PMID 37972095 DOI: 10.1073/pnas.2317221120 |
0.312 |
|
2023 |
Lukoyanov DA, Yang ZY, Shisler K, Peters JW, Raugei S, Dean DR, Seefeldt LC, Hoffman BM. A conformational equilibrium in the nitrogenase MoFe protein with an α-V70I amino acid substitution illuminates the mechanism of H formation. Faraday Discussions. PMID 37021412 DOI: 10.1039/d2fd00153e |
0.556 |
|
2023 |
Martin Del Campo JS, Rigsbee J, Bueno Batista M, Mus F, Rubio LM, Einsle O, Peters JW, Dixon R, Dean DR, Dos Santos PC. Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in . Critical Reviews in Biochemistry and Molecular Biology. 1-47. PMID 36877487 DOI: 10.1080/10409238.2023.2181309 |
0.47 |
|
2023 |
Yang ZY, Badalyan A, Hoffman BM, Dean DR, Seefeldt LC. The Fe Protein Cycle Associated with Nitrogenase Catalysis Requires the Hydrolysis of Two ATP for Each Single Electron Transfer Event. Journal of the American Chemical Society. PMID 36857604 DOI: 10.1021/jacs.2c09576 |
0.384 |
|
2022 |
Van Stappen C, Jiménez-Vicente E, Pérez-González A, Yang ZY, Seefeldt LC, DeBeer S, Dean DR, Decamps L. A conformational role for NifW in the maturation of molybdenum nitrogenase P-cluster. Chemical Science. 13: 3489-3500. PMID 35432878 DOI: 10.1039/d1sc06418e |
0.354 |
|
2022 |
Pérez-González A, Jimenez-Vicente E, Salinero-Lanzarote A, Harris DF, Seefeldt LC, Dean DR. AnfO controls fidelity of nitrogenase FeFe protein maturation by preventing misincorporation of FeV-cofactor. Molecular Microbiology. PMID 35220629 DOI: 10.1111/mmi.14890 |
0.351 |
|
2021 |
Pérez-González A, Jimenez-Vicente E, Gies-Elterlein J, Salinero-Lanzarote A, Yang ZY, Einsle O, Seefeldt LC, Dean DR. Specificity of NifEN and VnfEN for the Assembly of Nitrogenase Active Site Cofactors in Azotobacter vinelandii. Mbio. e0156821. PMID 34281397 DOI: 10.1128/mBio.01568-21 |
0.32 |
|
2021 |
Peters JW, Einsle O, Dean DR, DeBeer S, Hoffman BM, Holland PL, Seefeldt LC. Comment on "Structural evidence for a dynamic metallocofactor during N reduction by Mo-nitrogenase". Science (New York, N.Y.). 371. PMID 33574183 DOI: 10.1126/science.abe5481 |
0.518 |
|
2020 |
Seefeldt LC, Yang ZY, Lukoyanov DA, Harris DF, Dean DR, Raugei S, Hoffman BM. Reduction of Substrates by Nitrogenases. Chemical Reviews. PMID 32176472 DOI: 10.1021/Acs.Chemrev.9B00556 |
0.309 |
|
2019 |
Burén S, Pratt K, Jiang X, Guo Y, Jimenez-Vicente E, Echavarri-Erasun C, Dean DR, Saaem I, Gordon DB, Voigt CA, Rubio LM. Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co in . Proceedings of the National Academy of Sciences of the United States of America. PMID 31767756 DOI: 10.1073/Pnas.1904903116 |
0.464 |
|
2019 |
Lukoyanov D, Krzyaniak MD, Dean DR, Wasielewski MR, Seefeldt LC, Hoffman BM. Time-Resolved EPR Study of H Reductive Elimination from the Photoexcited Nitrogenase Janus E(4H) Intermediate. The Journal of Physical Chemistry. B. PMID 31549504 DOI: 10.1021/Acs.Jpcb.9B07776 |
0.336 |
|
2019 |
Harris D, Lukoyanov D, Kallas H, Trncik C, Yang ZY, Compton PD, Kelleher NL, Einsle O, Dean DR, Hoffman BM, Seefeldt LC. Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism to Achieve N Reduction. Biochemistry. PMID 31283201 DOI: 10.1021/Acs.Biochem.9B00468 |
0.409 |
|
2019 |
Jimenez-Vicente E, Yang ZY, Martin Del Campo JS, Cash VL, Seefeldt LC, Dean DR. The NifZ accessory protein has an equivalent function in maturation of both nitrogenase MoFe protein P-clusters. The Journal of Biological Chemistry. PMID 30846561 DOI: 10.1074/Jbc.Ra119.007905 |
0.463 |
|
2018 |
Jiménez-Vicente E, Martin Del Campo JS, Yang ZY, Cash VL, Dean DR, Seefeldt LC. Application of affinity purification methods for analysis of the nitrogenase system from Azotobacter vinelandii. Methods in Enzymology. 613: 231-255. PMID 30509468 DOI: 10.1016/Bs.Mie.2018.10.007 |
0.424 |
|
2018 |
Harris D, Yang Z, Dean DR, Seefeldt LC, Hoffman BM. Kinetic Understanding of N Reduction versus H Evolution at the E(4H) Janus State in the Three Nitrogenases. Biochemistry. PMID 30183278 DOI: 10.1021/Acs.Biochem.8B00784 |
0.349 |
|
2018 |
Seefeldt LC, Hoffman BM, Peters JW, Raugei S, Beratan DN, Antony E, Dean DR. Energy Transduction in Nitrogenase. Accounts of Chemical Research. PMID 30095253 DOI: 10.1021/Acs.Accounts.8B00112 |
0.626 |
|
2018 |
Jimenez-Vicente E, Yang ZY, Ray WK, Echavarri-Erasun C, Cash VL, Rubio LM, Seefeldt LC, Dean DR. Sequential and differential interaction of assembly factors during nitrogenase MoFe protein maturation. The Journal of Biological Chemistry. PMID 29724822 DOI: 10.1074/Jbc.Ra118.002994 |
0.453 |
|
2018 |
Lukoyanov DA, Khadka N, Yang ZY, Dean DR, Seefeldt LC, Hoffman BM. Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis. Inorganic Chemistry. PMID 29575898 DOI: 10.1021/Acs.Inorgchem.8B00271 |
0.356 |
|
2017 |
Harris D, Lukoyanov D, Shaw S, Compton PD, Tokmina-Lukaszewska M, Bothner B, Kelleher NL, Dean DR, Hoffman BM, Seefeldt LC. The Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2. Biochemistry. PMID 29283553 DOI: 10.1021/Acs.Biochem.7B01142 |
0.469 |
|
2017 |
Hu B, Harris DF, Dean DR, Liu TL, Yang ZY, Seefeldt LC. Electrocatalytic CO2 reduction catalyzed by nitrogenase MoFe and FeFe proteins. Bioelectrochemistry (Amsterdam, Netherlands). 120: 104-109. PMID 29223886 DOI: 10.1016/J.Bioelechem.2017.12.002 |
0.43 |
|
2017 |
Khadka N, Milton RD, Shaw S, Lukoyanov D, Dean DR, Minteer SD, Raugei S, Hoffman BM, Seefeldt LC. The Mechanism of Nitrogenase H2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects. Journal of the American Chemical Society. PMID 28851217 DOI: 10.1021/Jacs.7B07311 |
0.396 |
|
2017 |
Paengnakorn P, Ash PA, Shaw S, Danyal K, Chen T, Dean DR, Seefeldt LC, Vincent KA. Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding. Chemical Science. 8: 1500-1505. PMID 28616146 DOI: 10.1039/C6Sc02860H |
0.457 |
|
2016 |
Davydov R, Khadka N, Yang ZY, Fielding AJ, Lukoyanov D, Dean DR, Seefeldt LC, Hoffman BM. Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements. Israel Journal of Chemistry. 56: 841-851. PMID 27777444 DOI: 10.1002/Ijch.201600026 |
0.375 |
|
2016 |
Danyal K, Shaw S, Page TR, Duval S, Horitani M, Marts AR, Lukoyanov D, Dean DR, Raugei S, Hoffman BM, Seefeldt LC, Antony E. Negative cooperativity in the nitrogenase Fe protein electron delivery cycle. Proceedings of the National Academy of Sciences of the United States of America. 113: E5783-E5791. PMID 27698129 DOI: 10.1073/Pnas.1613089113 |
0.475 |
|
2016 |
Lukoyanov D, Khadka N, Yang ZY, Dean DR, Seefeldt LC, Hoffman BM. Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme. Journal of the American Chemical Society. PMID 27529724 DOI: 10.1021/Jacs.6B06362 |
0.373 |
|
2016 |
Khadka N, Dean DR, Smith D, Hoffman BM, Raugei S, Seefeldt LC. CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane. Inorganic Chemistry. PMID 27500789 DOI: 10.1021/Acs.Inorgchem.6B00388 |
0.397 |
|
2016 |
Yang ZY, Ledbetter R, Shaw S, Pence NK, Tokmina-Lukaszewska M, Eilers BJ, Guo Q, Pokhrel N, Cash VL, Dean DR, Antony E, Bothner B, Peters JW, Seefeldt LC. Evidence that the Pi Release Event is the Rate Limiting Step in the Nitrogenase Catalytic Cycle. Biochemistry. PMID 27295169 DOI: 10.1021/Acs.Biochem.6B00421 |
0.651 |
|
2016 |
Lukoyanov D, Khadka N, Yang ZY, Dean DR, Seefeldt LC, Hoffman BM. Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E4(4H) Janus Intermediate. Journal of the American Chemical Society. PMID 26788586 DOI: 10.1021/Jacs.5B11650 |
0.303 |
|
2016 |
Milton RD, Abdellaoui S, Khadka N, Dean DR, Leech D, Seefeldt LC, Minteer SD. Nitrogenase bioelectrocatalysis: Heterogeneous ammonia and hydrogen production by MoFe protein Energy and Environmental Science. 9: 2550-2554. DOI: 10.1039/C6Ee01432A |
0.437 |
|
2015 |
Dean DR, Dos Santos PC. Trading Places-Switching Frataxin Function by a Single Amino Acid Substitution within the [Fe-S] Cluster Assembly Scaffold. Plos Genetics. 11: e1005192. PMID 25996679 DOI: 10.1371/Journal.Pgen.1005192 |
0.492 |
|
2015 |
Danyal K, Rasmussen AJ, Keable SM, Inglet BS, Shaw S, Zadvornyy OA, Duval S, Dean DR, Raugei S, Peters JW, Seefeldt LC. Fe protein-independent substrate reduction by nitrogenase MoFe protein variants. Biochemistry. 54: 2456-62. PMID 25831270 DOI: 10.1021/Acs.Biochem.5B00140 |
0.661 |
|
2015 |
Lill R, Broderick JB, Dean DR. Special issue on iron-sulfur proteins: Structure, function, biogenesis and diseases. Biochimica Et Biophysica Acta. 1853: 1251-2. PMID 25746719 DOI: 10.1016/J.Bbamcr.2015.03.001 |
0.368 |
|
2015 |
Lukoyanov D, Yang ZY, Khadka N, Dean DR, Seefeldt LC, Hoffman BM. Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂. Journal of the American Chemical Society. 137: 3610-5. PMID 25741750 DOI: 10.1021/Jacs.5B00103 |
0.343 |
|
2014 |
Shaw S, Lukoyanov D, Danyal K, Dean DR, Hoffman BM, Seefeldt LC. Nitrite and hydroxylamine as nitrogenase substrates: mechanistic implications for the pathway of N₂ reduction. Journal of the American Chemical Society. 136: 12776-83. PMID 25136926 DOI: 10.1021/Ja507123D |
0.323 |
|
2014 |
Lukoyanov D, Yang ZY, Duval S, Danyal K, Dean DR, Seefeldt LC, Hoffman BM. A confirmation of the quench-cryoannealing relaxation protocol for identifying reduction states of freeze-trapped nitrogenase intermediates. Inorganic Chemistry. 53: 3688-93. PMID 24635454 DOI: 10.1021/Ic500013C |
0.413 |
|
2014 |
Dos Santos PC, Dean DR. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii Iron-Sulfur Clusters in Chemistry and Biology. 267-296. DOI: 10.1515/9783110308426.267 |
0.321 |
|
2013 |
Duval S, Danyal K, Shaw S, Lytle AK, Dean DR, Hoffman BM, Antony E, Seefeldt LC. Electron transfer precedes ATP hydrolysis during nitrogenase catalysis. Proceedings of the National Academy of Sciences of the United States of America. 110: 16414-9. PMID 24062462 DOI: 10.1073/Pnas.1311218110 |
0.428 |
|
2013 |
Yang ZY, Khadka N, Lukoyanov D, Hoffman BM, Dean DR, Seefeldt LC. On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase. Proceedings of the National Academy of Sciences of the United States of America. 110: 16327-32. PMID 24062454 DOI: 10.1073/Pnas.1315852110 |
0.365 |
|
2013 |
Seefeldt LC, Yang ZY, Duval S, Dean DR. Nitrogenase reduction of carbon-containing compounds. Biochimica Et Biophysica Acta. 1827: 1102-11. PMID 23597875 DOI: 10.1016/J.Bbabio.2013.04.003 |
0.303 |
|
2013 |
Hoffman BM, Lukoyanov D, Dean DR, Seefeldt LC. Nitrogenase: a draft mechanism. Accounts of Chemical Research. 46: 587-95. PMID 23289741 DOI: 10.1021/Ar300267M |
0.438 |
|
2013 |
Yamanaka Y, Zeppieri L, Nicolet Y, Marinoni EN, de Oliveira JS, Odaka M, Dean DR, Fontecilla-Camps JC. Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus. Dalton Transactions (Cambridge, England : 2003). 42: 3092-9. PMID 23160436 DOI: 10.1039/C2Dt32101G |
0.433 |
|
2012 |
Yang ZY, Moure VR, Dean DR, Seefeldt LC. Carbon dioxide reduction to methane and coupling with acetylene to form propylene catalyzed by remodeled nitrogenase. Proceedings of the National Academy of Sciences of the United States of America. 109: 19644-8. PMID 23150564 DOI: 10.1073/Pnas.1213159109 |
0.314 |
|
2012 |
Mayweather D, Danyal K, Dean DR, Seefeldt LC, Hoffman BM. Temperature invariance of the nitrogenase electron transfer mechanism. Biochemistry. 51: 8391-8. PMID 23050654 DOI: 10.1021/Bi301164J |
0.314 |
|
2012 |
George SJ, Barney BM, Mitra D, Igarashi RY, Guo Y, Dean DR, Cramer SP, Seefeldt LC. EXAFS and NRVS reveal a conformational distortion of the FeMo-cofactor in the MoFe nitrogenase propargyl alcohol complex. Journal of Inorganic Biochemistry. 112: 85-92. PMID 22564272 DOI: 10.1016/J.Jinorgbio.2012.02.004 |
0.423 |
|
2012 |
Lukoyanov D, Yang ZY, Barney BM, Dean DR, Seefeldt LC, Hoffman BM. Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase. Proceedings of the National Academy of Sciences of the United States of America. 109: 5583-7. PMID 22460797 DOI: 10.1073/Pnas.1202197109 |
0.355 |
|
2012 |
Seefeldt LC, Hoffman BM, Dean DR. Electron transfer in nitrogenase catalysis. Current Opinion in Chemical Biology. 16: 19-25. PMID 22397885 DOI: 10.1016/J.Cbpa.2012.02.012 |
0.452 |
|
2012 |
Liu Y, Dos Santos PC, Zhu X, Orlando R, Dean DR, Söll D, Yuan J. Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide. The Journal of Biological Chemistry. 287: 5426-33. PMID 22167197 DOI: 10.1074/Jbc.M111.313700 |
0.341 |
|
2011 |
Doan PE, Telser J, Barney BM, Igarashi RY, Dean DR, Seefeldt LC, Hoffman BM. 57Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple. Journal of the American Chemical Society. 133: 17329-40. PMID 21980917 DOI: 10.1021/Ja205304T |
0.46 |
|
2011 |
Danyal K, Dean DR, Hoffman BM, Seefeldt LC. Electron transfer within nitrogenase: evidence for a deficit-spending mechanism. Biochemistry. 50: 9255-63. PMID 21939270 DOI: 10.1021/Bi201003A |
0.47 |
|
2011 |
Lukoyanov D, Dikanov SA, Yang ZY, Barney BM, Samoilova RI, Narasimhulu KV, Dean DR, Seefeldt LC, Hoffman BM. ENDOR/HYSCORE studies of the common intermediate trapped during nitrogenase reduction of N2H2, CH3N2H, and N2H4 support an alternating reaction pathway for N2 reduction. Journal of the American Chemical Society. 133: 11655-64. PMID 21744838 DOI: 10.1021/Ja2036018 |
0.347 |
|
2011 |
Hamilton TL, Jacobson M, Ludwig M, Boyd ES, Bryant DA, Dean DR, Peters JW. Differential accumulation of nif structural gene mRNA in Azotobacter vinelandii. Journal of Bacteriology. 193: 4534-6. PMID 21725008 DOI: 10.1128/Jb.05100-11 |
0.758 |
|
2011 |
Hamilton TL, Ludwig M, Dixon R, Boyd ES, Dos Santos PC, Setubal JC, Bryant DA, Dean DR, Peters JW. Transcriptional profiling of nitrogen fixation in Azotobacter vinelandii. Journal of Bacteriology. 193: 4477-86. PMID 21724999 DOI: 10.1128/Jb.05099-11 |
0.761 |
|
2011 |
Yang ZY, Dean DR, Seefeldt LC. Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons. The Journal of Biological Chemistry. 286: 19417-21. PMID 21454640 DOI: 10.1074/Jbc.M111.229344 |
0.348 |
|
2011 |
Dos Santos PC, Dean DR. Co-ordination and fine-tuning of nitrogen fixation in Azotobacter vinelandii. Molecular Microbiology. 79: 1132-5. PMID 21338415 DOI: 10.1111/J.1365-2958.2011.07541.X |
0.35 |
|
2011 |
Yang ZY, Seefeldt LC, Dean DR, Cramer SP, George SJ. Steric control of the Hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopy. Angewandte Chemie (International Ed. in English). 50: 272-5. PMID 21120978 DOI: 10.1002/Anie.201005145 |
0.421 |
|
2010 |
Dos Santos PC, Dean DR. Bioinorganic chemistry: electrons in Fe-S protein assembly. Nature Chemical Biology. 6: 700-1. PMID 20852605 DOI: 10.1038/Nchembio.438 |
0.451 |
|
2010 |
Danyal K, Inglet BS, Vincent KA, Barney BM, Hoffman BM, Armstrong FA, Dean DR, Seefeldt LC. Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP. Journal of the American Chemical Society. 132: 13197-9. PMID 20812745 DOI: 10.1021/Ja1067178 |
0.485 |
|
2010 |
Danyal K, Mayweather D, Dean DR, Seefeldt LC, Hoffman BM. Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein. Journal of the American Chemical Society. 132: 6894-5. PMID 20429505 DOI: 10.1021/Ja101737F |
0.479 |
|
2010 |
Lukoyanov D, Yang ZY, Dean DR, Seefeldt LC, Hoffman BM. Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein? Journal of the American Chemical Society. 132: 2526-7. PMID 20121157 DOI: 10.1021/Ja910613M |
0.385 |
|
2010 |
Sarma R, Barney BM, Keable S, Dean DR, Seefeldt LC, Peters JW. Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70(Ile) MoFe protein variant. Journal of Inorganic Biochemistry. 104: 385-9. PMID 20022118 DOI: 10.1016/J.Jinorgbio.2009.11.009 |
0.567 |
|
2010 |
Brigle KE, Setterquist RA, Dean DR, Cantwell JS, Weiss MC, Newton WE. Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii. Proceedings of the National Academy of Sciences of the United States of America. 84: 7066-9. PMID 16593879 DOI: 10.1073/Pnas.84.20.7066 |
0.41 |
|
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 |
0.482 |
|
2009 |
Barney BM, Lukoyanov D, Igarashi RY, Laryukhin M, Yang TC, Dean DR, Hoffman BM, Seefeldt LC. Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase. Biochemistry. 48: 9094-102. PMID 19663502 DOI: 10.1021/Bi901092Z |
0.381 |
|
2009 |
Seefeldt LC, Hoffman BM, Dean DR. Mechanism of Mo-dependent nitrogenase. Annual Review of Biochemistry. 78: 701-22. PMID 19489731 DOI: 10.1146/Annurev.Biochem.78.070907.103812 |
0.496 |
|
2009 |
Barney BM, Yurth MG, Dos Santos PC, Dean DR, Seefeldt LC. A substrate channel in the nitrogenase MoFe protein. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 1015-22. PMID 19458968 DOI: 10.1007/S00775-009-0544-2 |
0.371 |
|
2009 |
Setubal JC, dos Santos P, Goldman BS, Ertesvåg H, Espin G, Rubio LM, Valla S, Almeida NF, Balasubramanian D, Cromes L, Curatti L, Du Z, Godsy E, Goodner B, Hellner-Burris K, ... ... Dean DR, et al. Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized to support diverse anaerobic metabolic processes. Journal of Bacteriology. 191: 4534-45. PMID 19429624 DOI: 10.1128/Jb.00504-09 |
0.737 |
|
2009 |
Hoffman BM, Dean DR, Seefeldt LC. Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation. Accounts of Chemical Research. 42: 609-19. PMID 19267458 DOI: 10.1021/Ar8002128 |
0.417 |
|
2008 |
Dos Santos PC, Dean DR. A newly discovered role for iron-sulfur clusters. Proceedings of the National Academy of Sciences of the United States of America. 105: 11589-90. PMID 18697949 DOI: 10.1073/Pnas.0805713105 |
0.489 |
|
2008 |
Raulfs EC, O'Carroll IP, Dos Santos PC, Unciuleac MC, Dean DR. In vivo iron-sulfur cluster formation. Proceedings of the National Academy of Sciences of the United States of America. 105: 8591-6. PMID 18562278 DOI: 10.1073/Pnas.0803173105 |
0.789 |
|
2008 |
Bandyopadhyay S, Naik SG, O'Carroll IP, Huynh BH, Dean DR, Johnson MK, Dos Santos PC. A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier. The Journal of Biological Chemistry. 283: 14092-9. PMID 18339629 DOI: 10.1074/Jbc.M709161200 |
0.794 |
|
2007 |
Lukoyanov D, Pelmenschikov V, Maeser N, Laryukhin M, Yang TC, Noodleman L, Dean DR, Case DA, Seefeldt LC, Hoffman BM. Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environments. Inorganic Chemistry. 46: 11437-49. PMID 18027933 DOI: 10.1021/Ic7018814 |
0.347 |
|
2007 |
Dos Santos PC, Mayer SM, Barney BM, Seefeldt LC, Dean DR. Alkyne substrate interaction within the nitrogenase MoFe protein. Journal of Inorganic Biochemistry. 101: 1642-8. PMID 17610955 DOI: 10.1016/J.Jinorgbio.2007.05.007 |
0.409 |
|
2007 |
Barney BM, McClead J, Lukoyanov D, Laryukhin M, Yang TC, Dean DR, Hoffman BM, Seefeldt LC. Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reduction. Biochemistry. 46: 6784-94. PMID 17508723 DOI: 10.1021/Bi062294S |
0.388 |
|
2007 |
Unciuleac MC, Chandramouli K, Naik S, Mayer S, Huynh BH, Johnson MK, Dean DR. In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry. 46: 6812-21. PMID 17506526 DOI: 10.1021/Bi6026665 |
0.465 |
|
2007 |
Chandramouli K, Unciuleac MC, Naik S, Dean DR, Huynh BH, Johnson MK. Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein. Biochemistry. 46: 6804-11. PMID 17506525 DOI: 10.1021/Bi6026659 |
0.463 |
|
2007 |
Frazzon AP, Ramirez MV, Warek U, Balk J, Frazzon J, Dean DR, Winkel BS. Functional analysis of Arabidopsis genes involved in mitochondrial iron-sulfur cluster assembly. Plant Molecular Biology. 64: 225-40. PMID 17417719 DOI: 10.1007/S11103-007-9147-X |
0.447 |
|
2007 |
Lukoyanov D, Barney BM, Dean DR, Seefeldt LC, Hoffman BM. Connecting nitrogenase intermediates with the kinetic scheme for N2 reduction by a relaxation protocol and identification of the N2 binding state. Proceedings of the National Academy of Sciences of the United States of America. 104: 1451-5. PMID 17251348 DOI: 10.1073/Pnas.0610975104 |
0.365 |
|
2007 |
Dos Santos PC, Johnson DC, Ragle BE, Unciuleac MC, Dean DR. Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. Journal of Bacteriology. 189: 2854-62. PMID 17237162 DOI: 10.1128/Jb.01734-06 |
0.497 |
|
2007 |
Hernandez JA, Igarashi RY, Soboh B, Curatti L, Dean DR, Ludden PW, Rubio LM. NifX and NifEN exchange NifB cofactor and the VK-cluster, a newly isolated intermediate of the iron-molybdenum cofactor biosynthetic pathway. Molecular Microbiology. 63: 177-92. PMID 17163967 DOI: 10.1111/J.1365-2958.2006.05514.X |
0.46 |
|
2006 |
Barney BM, Lukoyanov D, Yang TC, Dean DR, Hoffman BM, Seefeldt LC. A methyldiazene (HN=N-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism. Proceedings of the National Academy of Sciences of the United States of America. 103: 17113-8. PMID 17088552 DOI: 10.1073/Pnas.0602130103 |
0.347 |
|
2006 |
Johnson DC, Unciuleac MC, Dean DR. Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii. Journal of Bacteriology. 188: 7551-61. PMID 16936042 DOI: 10.1128/Jb.00596-06 |
0.452 |
|
2006 |
Barney BM, Lee HI, Dos Santos PC, Hoffman BM, Dean DR, Seefeldt LC. Breaking the N2 triple bond: insights into the nitrogenase mechanism. Dalton Transactions (Cambridge, England : 2003). 2277-84. PMID 16688314 DOI: 10.1039/B517633F |
0.331 |
|
2005 |
Lee HI, Sørlie M, Christiansen J, Yang TC, Shao J, Dean DR, Hales BJ, Hoffman BM. Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO. Journal of the American Chemical Society. 127: 15880-90. PMID 16277531 DOI: 10.1021/Ja054078X |
0.464 |
|
2005 |
Barney BM, Yang TC, Igarashi RY, Dos Santos PC, Laryukhin M, Lee HI, Hoffman BM, Dean DR, Seefeldt LC. Intermediates trapped during nitrogenase reduction of N triple bond N, CH3-N=NH, and H2N-NH2. Journal of the American Chemical Society. 127: 14960-1. PMID 16248599 DOI: 10.1021/Ja0539342 |
0.314 |
|
2005 |
Smith AD, Jameson GN, Dos Santos PC, Agar JN, Naik S, Krebs C, Frazzon J, Dean DR, Huynh BH, Johnson MK. NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein. Biochemistry. 44: 12955-69. PMID 16185064 DOI: 10.1021/Bi051257I |
0.467 |
|
2005 |
Smith AD, Frazzon J, Dean DR, Johnson MK. Role of conserved cysteines in mediating sulfur transfer from IscS to IscU. Febs Letters. 579: 5236-40. PMID 16165131 DOI: 10.1016/J.Febslet.2005.08.046 |
0.309 |
|
2005 |
Yang TC, Maeser NK, Laryukhin M, Lee HI, Dean DR, Seefeldt LC, Hoffman BM. The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen. Journal of the American Chemical Society. 127: 12804-5. PMID 16159266 DOI: 10.1021/Ja0552489 |
0.324 |
|
2005 |
Johnson DC, Dean DR, Smith AD, Johnson MK. Structure, function, and formation of biological iron-sulfur clusters. Annual Review of Biochemistry. 74: 247-81. PMID 15952888 DOI: 10.1146/Annurev.Biochem.74.082803.133518 |
0.502 |
|
2005 |
Barney BM, Laryukhin M, Igarashi RY, Lee HI, Dos Santos PC, Yang TC, Hoffman BM, Dean DR, Seefeldt LC. Trapping a hydrazine reduction intermediate on the nitrogenase active site. Biochemistry. 44: 8030-7. PMID 15924422 DOI: 10.1021/Bi0504409 |
0.407 |
|
2005 |
Igarashi RY, Laryukhin M, Dos Santos PC, Lee HI, Dean DR, Seefeldt LC, Hoffman BM. Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy. Journal of the American Chemical Society. 127: 6231-41. PMID 15853328 DOI: 10.1021/Ja043596P |
0.346 |
|
2005 |
Dos Santos PC, Igarashi RY, Lee HI, Hoffman BM, Seefeldt LC, Dean DR. Substrate interactions with the nitrogenase active site. Accounts of Chemical Research. 38: 208-14. PMID 15766240 DOI: 10.1021/Ar040050Z |
0.308 |
|
2005 |
Johnson DC, Dos Santos PC, Dean DR. NifU and NifS are required for the maturation of nitrogenase and cannot replace the function of isc-gene products in Azotobacter vinelandii. Biochemical Society Transactions. 33: 90-3. PMID 15667274 DOI: 10.1042/Bst0330090 |
0.476 |
|
2004 |
Barney BM, Igarashi RY, Dos Santos PC, Dean DR, Seefeldt LC. Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis. The Journal of Biological Chemistry. 279: 53621-4. PMID 15465817 DOI: 10.1074/Jbc.M410247200 |
0.406 |
|
2004 |
Lee HI, Igarashi RY, Laryukhin M, Doan PE, Dos Santos PC, Dean DR, Seefeldt LC, Hoffman BM. An organometallic intermediate during alkyne reduction by nitrogenase. Journal of the American Chemical Society. 126: 9563-9. PMID 15291559 DOI: 10.1021/Ja048714N |
0.389 |
|
2004 |
Igarashi RY, Dos Santos PC, Niehaus WG, Dance IG, Dean DR, Seefeldt LC. Localization of a catalytic intermediate bound to the FeMo-cofactor of nitrogenase. The Journal of Biological Chemistry. 279: 34770-5. PMID 15181010 DOI: 10.1074/Jbc.M403194200 |
0.376 |
|
2004 |
Dos Santos PC, Smith AD, Frazzon J, Cash VL, Johnson MK, Dean DR. Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein. The Journal of Biological Chemistry. 279: 19705-11. PMID 14993221 DOI: 10.1074/Jbc.M400278200 |
0.472 |
|
2004 |
Dos Santos PC, Dean DR, Hu Y, Ribbe MW. Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chemical Reviews. 104: 1159-73. PMID 14871152 DOI: 10.1021/Cr020608L |
0.328 |
|
2004 |
Seefeldt LC, Dance IG, Dean DR. Substrate interactions with nitrogenase: Fe versus Mo. Biochemistry. 43: 1401-9. PMID 14769015 DOI: 10.1021/Bi036038G |
0.393 |
|
2003 |
Benton PM, Laryukhin M, Mayer SM, Hoffman BM, Dean DR, Seefeldt LC. Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe protein. Biochemistry. 42: 9102-9. PMID 12885243 DOI: 10.1021/Bi034595X |
0.318 |
|
2003 |
Lee HI, Benton PM, Laryukhin M, Igarashi RY, Dean DR, Seefeldt LC, Hoffman BM. The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogen. Journal of the American Chemical Society. 125: 5604-5. PMID 12733878 DOI: 10.1021/Ja034383N |
0.328 |
|
2003 |
Frazzon J, Dean DR. Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Current Opinion in Chemical Biology. 7: 166-73. PMID 12714048 DOI: 10.1016/S1367-5931(03)00021-8 |
0.433 |
|
2003 |
Rüttimann-Johnson C, Rubio LM, Dean DR, Ludden PW. VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii. Journal of Bacteriology. 185: 2383-6. PMID 12644512 DOI: 10.1128/Jb.185.7.2383-2386.2003 |
0.323 |
|
2003 |
Huynh BH, Jameson GN, Smith AD, Johnson MK, Frazzon J, Dean DR, Krebs C. NifS-mediated assembly of [4Fe4S] clusters on NifU and homologous scaffold proteins Journal of Inorganic Biochemistry. 96: 80. DOI: 10.1016/S0162-0134(03)80539-1 |
0.382 |
|
2002 |
Frazzon J, Fick JR, Dean DR. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochemical Society Transactions. 30: 680-5. PMID 12196163 DOI: 10.1042/Bst0300680 |
0.509 |
|
2002 |
Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK. Structure of a cofactor-deficient nitrogenase MoFe protein. Science (New York, N.Y.). 296: 352-6. PMID 11951047 DOI: 10.1126/Science.1070010 |
0.574 |
|
2002 |
Mayer SM, Niehaus WG, Dean DR. Reduction of short chain alkynes by a nitrogenase α-70 Ala-substituted MoFe protein Dalton Transactions. 802-807. DOI: 10.1039/B107336B |
0.463 |
|
2002 |
Mayer SM, Niehaus WG, Dean DR. Reduction of short chain alkynes by a nitrogenase α-70Ala-substituted MoFe protein Journal of the Chemical Society, Dalton Transactions. 802-807. |
0.33 |
|
2001 |
Frazzon J, Dean DR. Feedback regulation of iron-sulfur cluster biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 98: 14751-3. PMID 11752417 DOI: 10.1073/Pnas.011579098 |
0.49 |
|
2001 |
Krebs C, Agar JN, Smith AD, Frazzon J, Dean DR, Huynh BH, Johnson MK. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry. 40: 14069-80. PMID 11705400 DOI: 10.1021/Bi015656Z |
0.487 |
|
2001 |
Benton PMC, Mayer SM, Shao J, Hoffman BM, Dean DR, Seefeldt LC. Interaction of acetylene and cyanide with the resting state of nitrogenase α-96-substituted MoFe proteins Biochemistry. 40: 13816-13825. PMID 11705370 DOI: 10.1021/Bi011571M |
0.402 |
|
2001 |
Benton PMC, Christiansen J, Dean DR, Seefeldt LC. Stereospecificity of acetylene reduction catalyzed by nitrogenase Journal of the American Chemical Society. 123: 1822-1827. PMID 11456800 DOI: 10.1021/Ja003662X |
0.308 |
|
2001 |
Sørlie M, Christiansen J, Lemon BJ, Peters JW, Dean DR, Hales BJ. Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein. Biochemistry. 40: 1540-9. PMID 11327812 DOI: 10.1021/Bi0013997 |
0.378 |
|
2000 |
Christiansen J, Chan JM, Seefeldt LC, Dean DR. The role of the MoFe protein alpha-125Phe and beta-125Phe residues in Azotobacter vinelandii MoFe protein-Fe protein interaction. Journal of Inorganic Biochemistry. 80: 195-204. PMID 11001089 DOI: 10.1016/S0162-0134(00)00083-0 |
0.441 |
|
2000 |
Christiansen J, Seefeldt LC, Dean DR. Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase Journal of Biological Chemistry. 275: 36104-36107. PMID 10948195 DOI: 10.1074/Jbc.M004889200 |
0.339 |
|
2000 |
Agar JN, Krebs C, Frazzon J, Huynh BH, Dean DR, Johnson MK. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry. 39: 7856-62. PMID 10891064 DOI: 10.1021/Bi000931N |
0.472 |
|
2000 |
Chan JM, Wu W, Dean DR, Seefeldt LC. Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis. Biochemistry. 39: 7221-8. PMID 10852721 DOI: 10.1021/Bi000219Q |
0.519 |
|
2000 |
Agar JN, Yuvaniyama P, Jack RF, Cash VL, Smith AD, Dean DR, Johnson MK. Modular organization and identification of a mononuclear iron-binding site within the NifU protein. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 167-77. PMID 10819462 DOI: 10.1007/S007750050361 |
0.51 |
|
2000 |
Christiansen J, Cash VL, Seefeldt LC, Dean DR. Isolation and characterization of an acetylene-resistant nitrogenase Journal of Biological Chemistry. 275: 11459-11464. PMID 10753963 DOI: 10.1074/Jbc.275.15.11459 |
0.379 |
|
2000 |
Yuvaniyama P, Agar JN, Cash VL, Johnson MK, Dean DR. NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 599-604. PMID 10639125 DOI: 10.1073/Pnas.97.2.599 |
0.483 |
|
2000 |
Lee HI, Sørlie M, Christiansen J, Song R, Dean DR, Hales BJ, Hoffman BM. Characterization of an intermediate in the reduction of acetylene by the nitrogenase α-Gln195 MoFe protein by Q-band EPR and 13C,1H ENDOR Journal of the American Chemical Society. 122: 5582-5587. DOI: 10.1021/Ja000542G |
0.341 |
|
2000 |
Foster MW, Yuvaniyami P, Cowan JA, Agar JN, Cash VL, Johnson MK, Dean DR. NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein Chemtracts. 13: 316-319. |
0.373 |
|
1999 |
Jung YS, Gao-Sheridan HS, Christiansen J, Dean DR, Burgess BK. Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein Journal of Biological Chemistry. 274: 32402-32410. PMID 10542283 DOI: 10.1074/Jbc.274.45.32402 |
0.514 |
|
1999 |
Rangaraj P, Ryle MJ, Lanzilotta WN, Goodwin PJ, Dean DR, Shah VK, Ludden PW. Inhibition of iron-molybdenum cofactor biosynthesis by L127Delta NifH and evidence for a complex formation between L127Delta NifH and NifNE. The Journal of Biological Chemistry. 274: 29413-9. PMID 10506203 DOI: 10.1074/Jbc.274.41.29413 |
0.349 |
|
1999 |
Chan JM, Christiansen J, Dean DR, Seefeldt LC. Spectroscopic evidence for changes in the redox state of the nitrogenase P-cluster during turnover. Biochemistry. 38: 5779-85. PMID 10231529 DOI: 10.1021/Bi982866B |
0.458 |
|
1998 |
Lee HI, Thrasher KS, Dean DR, Newton WE, Hoffman BM. 14N electron spin-echo envelope modulation of the S = 3/2 spin system of the Azotobacter vinelandii nitrogenase iron-molybdenum cofactor Biochemistry. 37: 13370-13378. PMID 9748344 DOI: 10.1021/Bi980956A |
0.348 |
|
1998 |
Christiansen J, Goodwin PJ, Lanzilotta WN, Seefeldt LC, Dean DR. Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii Biochemistry. 37: 12611-12623. PMID 9730834 DOI: 10.1021/Bi981165B |
0.464 |
|
1998 |
Lanzilotta WN, Christiansen J, Dean DR, Seefeldt LC. Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenase Biochemistry. 37: 11376-11384. PMID 9698385 DOI: 10.1021/Bi980048D |
0.401 |
|
1998 |
Goodwin PJ, Agar JN, Roll JT, Roberts GP, Johnson MK, Dean DR. The Azotobacter vinelandii NifEN complex contains two identical [4Fe-4S] clusters. Biochemistry. 37: 10420-8. PMID 9671511 DOI: 10.1021/Bi980435N |
0.455 |
|
1998 |
Zheng L, Cash VL, Flint DH, Dean DR. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii Journal of Biological Chemistry. 273: 13264-13272. PMID 9582371 DOI: 10.1074/Jbc.273.21.13264 |
0.408 |
|
1997 |
Chen S, Zheng L, Dean DR, Zalkin H. Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase Journal of Bacteriology. 179: 7587-7590. PMID 9393728 DOI: 10.1128/Jb.179.23.7587-7590.1997 |
0.445 |
|
1997 |
Shen J, Dean DR, Newton WE. Evidence for multiple substrate-reduction sites and distinct inhibitor- binding sites from an altered Azotobacter vinelandii nitrogenase MoFe protein Biochemistry. 36: 4884-4894. PMID 9125509 DOI: 10.1021/Bi9628578 |
0.386 |
|
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 |
0.603 |
|
1997 |
Seefeldt LC, Dean DR. Role of Nucleotides in Nitrogenase Catalysis Accounts of Chemical Research. 30: 260-266. DOI: 10.1007/0-306-47615-0_4 |
0.358 |
|
1995 |
Peters JW, Fisher K, Dean DR. Nitrogenase structure and function: A biochemical-genetic perspective Annual Review of Microbiology. 49: 335-366. PMID 8561464 DOI: 10.1146/Annurev.Mi.49.100195.002003 |
0.457 |
|
1995 |
DeRose VJ, Kim CH, Newton WE, Dean DR, Hoffman BM. Electron spin echo envelope modulation spectroscopic analysis of altered nitrogenase MoFe proteins from Azotobacter vinelandii. Biochemistry. 34: 2809-14. PMID 7893692 DOI: 10.1021/Bi00009A009 |
0.301 |
|
1995 |
Kim CH, Newton WE, Dean DR. Role of the MoFe protein α-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis Biochemistry. 34: 2798-2808. PMID 7893691 DOI: 10.1021/Bi00009A008 |
0.456 |
|
1995 |
Roll JT, Shah VK, Dean DR, Roberts GP. Characteristics of NIFNE in Azotobacter vinelandii strains: Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenase Journal of Biological Chemistry. 270: 4432-4437. PMID 7876209 DOI: 10.1074/Jbc.270.9.4432 |
0.355 |
|
1995 |
Peters JW, Fisher K, Newton WE, Dean DR. Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein Journal of Biological Chemistry. 270: 27007-27013. PMID 7592949 DOI: 10.1074/Jbc.270.45.27007 |
0.494 |
|
1995 |
Homer MJ, Dean DR, Roberts GP. Characterization of the gamma protein and its involvement in the metallocluster assembly and maturation of dinitrogenase from Azotobacter vinelandii. The Journal of Biological Chemistry. 270: 24745-52. PMID 7559591 DOI: 10.1074/Jbc.270.42.24745 |
0.423 |
|
1995 |
Finnegan M, Cantwell J, Fisher K, Dean D, Newton W, Johnson M. Modification of the properties of nitrogenase P-clusters via site-directed mutagenesis of coordinating residues Journal of Inorganic Biochemistry. 59: 559. DOI: 10.1016/0162-0134(95)97654-9 |
0.33 |
|
1995 |
DeRose VJ, Kim C, Peters JW, Newton WE, Dean DR, Hoffman BM. Site-specific mutations of the nitrogenase MoFe protein: ESEEM and ENDOR spectroscopic analyses of amino acid substitutions near to the FeMo-cofactor Journal of Inorganic Biochemistry. 59: 550. DOI: 10.1016/0162-0134(95)97645-7 |
0.304 |
|
1995 |
Dean DR. Biosynthesis of the nitrogenase iron-molybdenum cofactor Journal of Inorganic Biochemistry. 59: 97. DOI: 10.1016/0162-0134(95)97207-7 |
0.322 |
|
1994 |
Zheng L, White RH, Cash VL, Dean DR. Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry. 33: 4714-20. PMID 8161529 DOI: 10.1021/Bi00181A031 |
0.375 |
|
1994 |
Zheng L, Dean DR. Catalytic formation of a nitrogenase iron-sulfur cluster Journal of Biological Chemistry. 269: 18723-18726. PMID 8034623 |
0.43 |
|
1994 |
Peters JW, Fisher K, Dean DR. Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein Journal of Biological Chemistry. 269: 28076-28083. PMID 7961744 |
0.375 |
|
1993 |
Zheng L, White RH, Cash VL, Jack RF, Dean DR. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 90: 2754-8. PMID 8464885 DOI: 10.1073/Pnas.90.7.2754 |
0.428 |
|
1993 |
Newton W, Kim C, Shen J, Cantwell J, Dean D. Altered nitrogenase MoFe proteins: Probes for the catalytic function of prosthetic groups. Journal of Inorganic Biochemistry. 51: 354. DOI: 10.1016/0162-0134(93)85385-L |
0.313 |
|
1992 |
Kennedy C, Dean D. The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii Molecular Genetics and Genomics. 231: 494-498. PMID 1538703 DOI: 10.1007/Bf00292722 |
0.334 |
|
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 |
0.508 |
|
1992 |
Seefeldt LC, Morgan TV, Dean DR, Mortenson LE. Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction Journal of Biological Chemistry. 267: 6680-6688. PMID 1313018 |
0.335 |
|
1991 |
Wang SZ, Dean DR, Chen JS, Johnson JL. The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum Journal of Bacteriology. 173: 3041-3046. PMID 2022611 DOI: 10.1128/Jb.173.10.3041-3046.1991 |
0.309 |
|
1991 |
May HD, Dean DR, Newton WE. Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the β-subunit Biochemical Journal. 277: 457-464. PMID 1650185 DOI: 10.1042/Bj2770457 |
0.425 |
|
1991 |
Thomann H, Bernardo M, Newton WE, Dean DR. N coordination of FeMo cofactor requires His-195 of the MoFe protein α subunit and is essential for biological nitrogen fixation Proceedings of the National Academy of Sciences of the United States of America. 88: 6620-6623. DOI: 10.1073/Pnas.88.15.6620 |
0.409 |
|
1990 |
Hinton SM, Dean D. Biogenesis of molybdenum cofactors Critical Reviews in Microbiology. 17: 169-188. PMID 2405878 DOI: 10.3109/10408419009105724 |
0.311 |
|
1990 |
Dean DR, Setterquist RA, Brigle KE, Scott DJ, Laird NF, Newton WE. Evidence that conserved residues Cys-62 and Cys-154 within the Azotobacter vinelandii nitrogenase MoFe protein alpha-subunit are essential for nitrogenase activity but conserved residues His-83 and Cys-88 are not. Molecular Microbiology. 4: 1505-12. PMID 2287275 DOI: 10.1111/J.1365-2958.1990.Tb02061.X |
0.457 |
|
1990 |
Jacobson MR, Cantwell JS, Dean DR. A hybrid Azotobacter vinelandii-Clostridium pasteurianum nitrogenase iron protein that has in vivo and in vitro catalytic activity. The Journal of Biological Chemistry. 265: 19429-33. PMID 2246234 |
0.388 |
|
1990 |
MartÃn AE, Burgess BK, Stout CD, Cash VL, Dean DR, Jensen GM, Stephens PJ. Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement. Proceedings of the National Academy of Sciences of the United States of America. 87: 598-602. PMID 2153958 DOI: 10.1073/Pnas.87.2.598 |
0.492 |
|
1990 |
Scott DJ, May HD, Newton WE, Brigle KE, Dean DR. Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis Nature. 343: 188-190. PMID 2153269 DOI: 10.1038/343188A0 |
0.474 |
|
1989 |
Martin AE, Burgess BK, Iismaa SE, Smartt CT, Jacobson MR, Dean DR. Construction and characterization of an Azotobacter vinelandii strain with mutations in the genes encoding flavodoxin and ferredoxin I. Journal of Bacteriology. 171: 3162-7. PMID 2722744 DOI: 10.1128/Jb.171.6.3162-3167.1989 |
0.343 |
|
1989 |
Jacobson MR, Brigle KE, Bennett LT, Setterquist RA, Wilson MS, Cash VL, Beynon J, Newton WE, Dean DR. Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii. Journal of Bacteriology. 171: 1017-27. PMID 2644218 DOI: 10.1128/Jb.171.2.1017-1027.1989 |
0.345 |
|
1989 |
Jacobson MR, Cash VL, Weiss MC, Laird NF, Newton WE, Dean DR. Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. Molecular & General Genetics : Mgg. 219: 49-57. PMID 2615765 DOI: 10.1007/Bf00261156 |
0.454 |
|
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 Journal of Biological Chemistry. 264: 11270-11274. DOI: 10.1016/s0021-9258(18)60459-4 |
0.375 |
|
1989 |
Burgess B, Martin A, Iismaa S, Stout C, Cash V, Dean D, Jensen G, Stephens P. Site directed mutagenesis of Azotobacter vinelandii ferredoxin I: [FeS] cluster driven protein rearrangement Journal of Inorganic Biochemistry. 36: 229. DOI: 10.1016/0162-0134(89)84244-8 |
0.473 |
|
1988 |
Bennett LT, Cannon F, Dean DR. Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter vinelandii Molecular Microbiology. 2: 315-321. PMID 2840552 DOI: 10.1111/J.1365-2958.1988.Tb00034.X |
0.329 |
|
1987 |
Robinson AC, Dean DR, Burgess BK. Iron-molybdenum cofactor biosynthesis in Azotobacter vinelandii requires the iron protein of nitrogenase Journal of Biological Chemistry. 262: 14327-14332. PMID 3477546 |
0.395 |
|
1987 |
Brigle KE, Weiss MC, Newton WE, Dean DR. Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK. Journal of Bacteriology. 169: 1547-1553. PMID 3470285 DOI: 10.1128/Jb.169.4.1547-1553.1987 |
0.412 |
|
1986 |
Bishop PE, Premakumar R, Dean DR, Jacobson MR, Chisnell JR, Rizzo TM, Kopczynski J. Nitrogen Fixation by Azotobacter vinelandii Strains Having Deletions in Structural Genes for Nitrogenase. Science (New York, N.Y.). 232: 92-4. PMID 17774003 DOI: 10.1126/Science.232.4746.92 |
0.315 |
|
1986 |
Robinson AC, Burgess BK, Dean DR. Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster Journal of Bacteriology. 166: 180-186. PMID 3457004 DOI: 10.1128/Jb.166.1.180-186.1986 |
0.469 |
|
1985 |
Dean DR, Brigle KE. Azotobacter vinelandii nifD- and nifE-encoded polypeptides share structural homology Proceedings of the National Academy of Sciences of the United States of America. 82: 5720-5723. PMID 16593596 DOI: 10.1073/Pnas.82.17.5720 |
0.316 |
|
1985 |
Brigle KE, Newton WE, Dean DR. Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster. Gene. 37: 37-44. PMID 3863780 DOI: 10.1016/0378-1119(85)90255-0 |
0.395 |
|
1983 |
Cerretti DP, Dean D, Davis GR, Bedwell DM, Nomura M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Research. 11: 2599-616. PMID 6222285 DOI: 10.1093/Nar/11.9.2599 |
0.35 |
|
1982 |
Nomura M, Dean D, Yates JL. Feedback regulation of ribosomal protein synthesis in Escherichia coli Trends in Biochemical Sciences. 7: 92-95. DOI: 10.1016/0968-0004(82)90154-2 |
0.352 |
|
1981 |
Dean D, Yates JL, Nomura M. Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli Cell. 24: 413-419. PMID 7016341 DOI: 10.1016/0092-8674(81)90331-7 |
0.33 |
|
1981 |
Dean D, Yates JL, Nomura M. Escherichia coli ribosomal protein S8 feedback regulates part of spc operon Nature. 289: 89-91. PMID 6450328 DOI: 10.1038/289089A0 |
0.334 |
|
1980 |
Nomura M, Yates JL, Dean D, Post LE. Feedback regulation of ribosomal protein gene expression in Escherichia coli: Structural homology of ribosomal RNA and ribosomal protein mRNA Proceedings of the National Academy of Sciences of the United States of America. 77: 7084-7088. PMID 7012833 DOI: 10.1073/Pnas.77.12.7084 |
0.36 |
|
1980 |
Dean D, Nomura M. Feedback regulation of ribosomal protein gene expression in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 77: 3590-3594. PMID 6251471 DOI: 10.1073/Pnas.77.6.3590 |
0.327 |
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