| Year |
Citation |
Score |
| 2023 |
Abi Ghaida F, Brinkert K, Chen P, DeBeer S, Hoffman BM, Holland PL, Laxmi S, MacFarlane D, Peters JC, Peters JW, Pickett CJ, Seefeldt LC, Shylin SI, Stephens IEL, Vincent KA, et al. Enzymatic N activation: general discussion. Faraday Discussions. PMID 37358386 DOI: 10.1039/d3fd90011h |
0.581 |
|
| 2023 |
Chen T, Ash PA, Seefeldt LC, Vincent KA. Electrochemical experiments define potentials associated with binding of substrates and inhibitors to nitrogenase MoFe protein. Faraday Discussions. PMID 37060162 DOI: 10.1039/d2fd00170e |
0.661 |
|
| 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 |
0.326 |
|
| 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 |
0.31 |
|
| 2021 |
Huang Q, Tokmina-Lukaszewska M, Johnson LE, Kallas H, Ginovska B, Peters JW, Seefeldt LC, Bothner B, Raugei S. Mechanical coupling in the nitrogenase complex. Plos Computational Biology. 17: e1008719. PMID 33661889 DOI: 10.1371/journal.pcbi.1008719 |
0.302 |
|
| 2020 |
Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice J, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti SS, Bennett B, Bothner B, Ando N, Antony E. The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and relieved upon ATP binding. The Journal of Biological Chemistry. 100107. PMID 33434584 DOI: 10.1074/jbc.RA120.016278 |
0.314 |
|
| 2020 |
Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice J, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti SS, Bennett B, Bothner B, Ando N, Antony E. The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and relieved upon ATP binding. The Journal of Biological Chemistry. PMID 33219127 DOI: 10.1074/jbc.RA120.016278 |
0.314 |
|
| 2020 |
Chica B, Ruzicka J, Kallas H, Mulder DW, Brown KA, Peters JW, Seefeldt LC, Dukovic G, King PW. Defining Intermediates of Nitrogenase MoFe Protein during N Reduction under Photochemical Electron Delivery from CdS Quantum Dots. Journal of the American Chemical Society. PMID 32787260 DOI: 10.1021/Jacs.0C06343 |
0.395 |
|
| 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 |
0.382 |
|
| 2020 |
Brown KA, Ruzicka J, Kallas H, Chica B, Mulder DW, Peters JW, Seefeldt LC, Dukovic G, King PW. Excitation-Rate Determines Product Stoichiometry in Photochemical Ammonia Production by CdS Quantum Dot-Nitrogenase MoFe Protein Complexes Acs Catalysis. DOI: 10.1021/Acscatal.0C02933 |
0.384 |
|
| 2019 |
Badalyan A, Yang ZY, Hu B, Luo J, Hu M, Liu T, Seefeldt LC. An Efficient Viologen-Based Electron Donor to Nitrogenase. Biochemistry. PMID 31682410 DOI: 10.1021/Acs.Biochem.9B00844 |
0.349 |
|
| 2019 |
Hickey DP, Cai R, Yang ZY, Grunau K, Einsle O, Seefeldt LC, Minteer SD. Establishing a Thermodynamic Landscape for the Active Site of Mo-Dependent Nitrogenase. Journal of the American Chemical Society. PMID 31577428 DOI: 10.1021/Jacs.9B06546 |
0.423 |
|
| 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 |
0.349 |
|
| 2019 |
Soundararajan M, Ledbetter R, Kusuma P, Zhen S, Ludden P, Bugbee B, Ensign SA, Seefeldt LC. Phototrophic N and CO Fixation Using a -H Mediated Electrochemical System With Infrared Photons. Frontiers in Microbiology. 10: 1817. PMID 31474945 DOI: 10.3389/Fmicb.2019.01817 |
0.322 |
|
| 2019 |
Van Stappen C, Davydov R, Yang ZY, Fan R, Guo Y, Bill E, Seefeldt LC, Hoffman BM, DeBeer S. Spectroscopic Description of the E State of Mo Nitrogenase Based on Mo and Fe X-ray Absorption and Mössbauer Studies. Inorganic Chemistry. PMID 31441651 DOI: 10.1021/Acs.Inorgchem.9B01951 |
0.426 |
|
| 2019 |
Hoeke V, Tociu L, Case DA, Seefeldt LC, Raugei S, Hoffman BM. High-Resolution ENDOR Spectroscopy Combined with Quantum Chemical Calculations Reveals the Structure of Nitrogenase Janus Intermediate E(4H). Journal of the American Chemical Society. PMID 31310109 DOI: 10.1021/Jacs.9B04474 |
0.391 |
|
| 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 |
0.437 |
|
| 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 |
0.375 |
|
| 2019 |
Moure VR, Siöberg CLB, Valdameri G, Nji E, Oliveira MAS, Gerdhardt ECM, Pedrosa FO, Mitchell DA, Seefeldt LC, Huergo LF, Högbom M, Nordlund S, Souza EM. The ammonium transporter AmtB and the PII signal transduction protein GlnZ are required to inhibit DraG in Azospirillum brasilense. The Febs Journal. PMID 30633437 DOI: 10.1111/Febs.14745 |
0.35 |
|
| 2019 |
Hu B, Hu M, Seefeldt L, Liu TL. Electrochemical Dinitrogen Reduction to Ammonia by Mo2N: Catalysis or Decomposition? Acs Energy Letters. 4: 1053-1054. DOI: 10.1021/Acsenergylett.9B00648 |
0.333 |
|
| 2019 |
Badalyan A, Yang Z, Seefeldt LC. A Voltammetric Study of Nitrogenase Catalysis Using Electron Transfer Mediators Acs Catalysis. 9: 1366-1372. DOI: 10.1021/Acscatal.8B04290 |
0.377 |
|
| 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 |
0.399 |
|
| 2018 |
Raugei S, Seefeldt LC, Hoffman BM. Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N reduction. Proceedings of the National Academy of Sciences of the United States of America. PMID 30355772 DOI: 10.1073/Pnas.1810211115 |
0.413 |
|
| 2018 |
Seefeldt LC, Peters JW, Beratan DN, Bothner B, Minteer SD, Raugei S, Hoffman BM. Control of electron transfer in nitrogenase. Current Opinion in Chemical Biology. 47: 54-59. PMID 30205289 DOI: 10.1016/J.Cbpa.2018.08.011 |
0.328 |
|
| 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 |
0.383 |
|
| 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 |
0.422 |
|
| 2018 |
Peters JW, Beratan DN, Bothner B, Dyer RB, Harwood CS, Heiden ZM, Hille R, Jones AK, King PW, Lu Y, Lubner CE, Minteer SD, Mulder DW, Raugei S, Schut GJ, ... Seefeldt LC, et al. A new era for electron bifurcation. Current Opinion in Chemical Biology. 47: 32-38. PMID 30077080 DOI: 10.1016/J.Cbpa.2018.07.026 |
0.327 |
|
| 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 |
0.385 |
|
| 2018 |
Mus F, Alleman AB, Pence N, Seefeldt LC, Peters JW. Exploring the alternatives of biological nitrogen fixation. Metallomics : Integrated Biometal Science. PMID 29629463 DOI: 10.1039/C8Mt00038G |
0.361 |
|
| 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 |
0.363 |
|
| 2018 |
Poudel S, Colman DR, Fixen KR, Ledbetter RN, Zheng Y, Pence N, Seefeldt LC, Peters JW, Harwood CS, Boyd ES. Electron transfer to nitrogenase in different genomic and metabolic backgrounds. Journal of Bacteriology. PMID 29483165 DOI: 10.1128/Jb.00757-17 |
0.344 |
|
| 2018 |
Zheng Y, Harris DF, Yu Z, Fu Y, Poudel S, Ledbetter RN, Fixen KR, Yang ZY, Boyd ES, Lidstrom ME, Seefeldt LC, Harwood CS. A pathway for biological methane production using bacterial iron-only nitrogenase. Nature Microbiology. PMID 29335552 DOI: 10.1038/S41564-017-0091-5 |
0.341 |
|
| 2018 |
Mao Z, Liou SH, Khadka N, Jenney FE, Goodin DB, Seefeldt LC, Adams MWW, Cramer S, Larsen DS. Cluster Dependent Charge-Transfer Dynamics in Iron-Sulfur Proteins. Biochemistry. PMID 29303562 DOI: 10.1021/Acs.Biochem.7B01159 |
0.378 |
|
| 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 |
0.466 |
|
| 2017 |
Keable SM, Vertemara J, Zadvornyy OA, Eilers BJ, Danyal K, Rasmussen AJ, De Gioia L, Zampella G, Seefeldt LC, Peters JW. Structural characterization of the nitrogenase molybdenum-iron protein with the substrate acetylene trapped near the active site. Journal of Inorganic Biochemistry. 180: 129-134. PMID 29275221 DOI: 10.1016/J.Jinorgbio.2017.12.008 |
0.468 |
|
| 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 |
0.411 |
|
| 2017 |
Garcia Costas AM, Poudel S, Miller AF, Schut GJ, Ledbetter RN, Fixen KR, Seefeldt LC, Adams MWW, Harwood CS, Boyd ES, Peters JW. Defining Electron Bifurcation in the Electron Transferring Flavoprotein Family. Journal of Bacteriology. PMID 28808132 DOI: 10.1128/Jb.00440-17 |
0.351 |
|
| 2017 |
Pence N, Tokmina-Lukaszewska M, Yang ZY, Ledbetter RN, Seefeldt LC, Bothner B, Peters JW. Unraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycle. The Journal of Biological Chemistry. PMID 28784660 DOI: 10.1074/Jbc.M117.801548 |
0.428 |
|
| 2017 |
Ledbetter R, Garcia-Costas AM, Lubner CE, Mulder DW, Tokmina-Lukaszewska M, Artz JH, Patterson A, Magnuson T, Jay ZJ, Duan HD, Miller J, Plunkett MH, Hoben JP, Barney BM, Carlson RP, ... ... Seefeldt LC, et al. The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis. Biochemistry. PMID 28704608 DOI: 10.1021/Acs.Biochem.7B00389 |
0.361 |
|
| 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 |
0.437 |
|
| 2017 |
Lukoyanov D, Khadka N, Dean DR, Raugei S, Seefeldt LC, Hoffman BM. Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate. Inorganic Chemistry. PMID 28177622 DOI: 10.1021/Acs.Inorgchem.6B02899 |
0.323 |
|
| 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 |
0.377 |
|
| 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 |
0.427 |
|
| 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 |
0.405 |
|
| 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 |
0.412 |
|
| 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 |
0.44 |
|
| 2016 |
Brown KA, Harris DF, Wilker MB, Rasmussen A, Khadka N, Hamby H, Keable S, Dukovic G, Peters JW, Seefeldt LC, King PW. Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid. Science (New York, N.Y.). 352: 448-50. PMID 27102481 DOI: 10.1126/Science.Aaf2091 |
0.385 |
|
| 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 |
0.332 |
|
| 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 |
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 |
0.447 |
|
| 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 |
0.385 |
|
| 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 |
0.371 |
|
| 2014 |
Willis RM, McCurdy AT, Ogborn MK, Wahlen BD, Quinn JC, Pease LF, Seefeldt LC. Improving energetics of triacylglyceride extraction from wet oleaginous microbes. Bioresource Technology. 167: 416-24. PMID 25000397 DOI: 10.1016/J.Biortech.2014.06.013 |
0.74 |
|
| 2014 |
Smith D, Danyal K, Raugei S, Seefeldt LC. Substrate channel in nitrogenase revealed by a molecular dynamics approach. Biochemistry. 53: 2278-85. PMID 24654842 DOI: 10.1021/Bi401313J |
0.329 |
|
| 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 |
0.417 |
|
| 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 |
0.41 |
|
| 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 |
0.393 |
|
| 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 |
0.343 |
|
| 2013 |
Adams C, Godfrey V, Wahlen B, Seefeldt L, Bugbee B. Understanding precision nitrogen stress to optimize the growth and lipid content tradeoff in oleaginous green microalgae. Bioresource Technology. 131: 188-94. PMID 23347926 DOI: 10.1016/J.Biortech.2012.12.143 |
0.712 |
|
| 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 |
0.464 |
|
| 2013 |
Moure VR, Danyal K, Yang ZY, Wendroth S, Müller-Santos M, Pedrosa FO, Scarduelli M, Gerhardt EC, Huergo LF, Souza EM, Seefeldt LC. The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB. Journal of Bacteriology. 195: 279-86. PMID 23144248 DOI: 10.1128/Jb.01517-12 |
0.436 |
|
| 2013 |
Wahlen BD, Morgan MR, McCurdy AT, Willis RM, Morgan MD, Dye DJ, Bugbee B, Wood BD, Seefeldt LC. Biodiesel from microalgae, yeast, and bacteria: Engine performance and exhaust emissions Energy and Fuels. 27: 220-228. DOI: 10.1021/Ef3012382 |
0.739 |
|
| 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 |
0.334 |
|
| 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 |
0.311 |
|
| 2012 |
Barney BM, Wahlen BD, Garner E, Wei J, Seefeldt LC. Differences in substrate specificities of five bacterial wax ester synthases. Applied and Environmental Microbiology. 78: 5734-45. PMID 22685145 DOI: 10.1128/Aem.00534-12 |
0.744 |
|
| 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 |
0.715 |
|
| 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 |
0.398 |
|
| 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 |
0.431 |
|
| 2011 |
Willis RM, Wahlen BD, Seefeldt LC, Barney BM. Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: a bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol. Biochemistry. 50: 10550-8. PMID 22035211 DOI: 10.1021/Bi2008646 |
0.769 |
|
| 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 |
0.742 |
|
| 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 |
0.401 |
|
| 2011 |
Danyal K, Yang ZY, Seefeldt LC. Electron paramagnetic resonance spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 766: 191-205. PMID 21833869 DOI: 10.1007/978-1-61779-194-9_13 |
0.361 |
|
| 2011 |
Yang ZY, Danyal K, Seefeldt LC. Mechanism of Mo-dependent nitrogenase. Methods in Molecular Biology (Clifton, N.J.). 766: 9-29. PMID 21833858 DOI: 10.1007/978-1-61779-194-9_2 |
0.322 |
|
| 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 |
0.383 |
|
| 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 |
0.395 |
|
| 2011 |
Wahlen BD, Willis RM, Seefeldt LC. Biodiesel production by simultaneous extraction and conversion of total lipids from microalgae, cyanobacteria, and wild mixed-cultures. Bioresource Technology. 102: 2724-30. PMID 21123059 DOI: 10.1016/J.Biortech.2010.11.026 |
0.755 |
|
| 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 |
0.413 |
|
| 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 |
0.708 |
|
| 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 |
0.442 |
|
| 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 |
0.397 |
|
| 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 |
0.344 |
|
| 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 |
0.73 |
|
| 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 |
0.476 |
|
| 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 |
0.389 |
|
| 2009 |
Wahlen BD, Oswald WS, Seefeldt LC, Barney BM. Purification, characterization, and potential bacterial wax production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8. Applied and Environmental Microbiology. 75: 2758-64. PMID 19270127 DOI: 10.1128/Aem.02578-08 |
0.761 |
|
| 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 |
0.45 |
|
| 2008 |
Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW. Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein. Biochemistry. 47: 13004-15. PMID 19006326 DOI: 10.1021/Bi801058R |
0.437 |
|
| 2008 |
Wahlen BD, Barney BM, Seefeldt LC. Synthesis of biodiesel from mixed feedstocks and longer chain alcohols using an acid-catalyzed method Energy and Fuels. 22: 4223-4228. DOI: 10.1021/Ef800279T |
0.733 |
|
| 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 |
0.354 |
|
| 2007 |
Sarma R, Mulder DW, Brecht E, Szilagyi RK, Seefeldt LC, Tsuruta H, Peters JW. Probing the MgATP-bound conformation of the nitrogenase Fe protein by solution small-angle X-ray scattering. Biochemistry. 46: 14058-66. PMID 18001132 DOI: 10.1021/Bi700446S |
0.402 |
|
| 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 |
0.429 |
|
| 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 |
0.425 |
|
| 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 |
0.405 |
|
| 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 |
0.384 |
|
| 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 |
0.386 |
|
| 2006 |
Sen S, Krishnakumar A, McClead J, Johnson MK, Seefeldt LC, Szilagyi RK, Peters JW. Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: Structural characterization of the nitrogenase Fe protein Leu127 deletion variant with bound MgATP. Journal of Inorganic Biochemistry. 100: 1041-52. PMID 16616373 DOI: 10.1016/J.Jinorgbio.2006.02.016 |
0.436 |
|
| 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 |
0.704 |
|
| 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 |
0.347 |
|
| 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 |
0.74 |
|
| 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 |
0.701 |
|
| 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 |
0.682 |
|
| 2004 |
Jang SB, Jeong MS, Seefeldt LC, Peters JW. Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 1028-33. PMID 15549494 DOI: 10.1007/S00775-004-0605-5 |
0.435 |
|
| 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 |
0.736 |
|
| 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 |
0.725 |
|
| 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 |
0.73 |
|
| 2004 |
Sen S, Igarashi R, Smith A, Johnson MK, Seefeldt LC, Peters JW. A conformational mimic of the MgATP-bound "on state" of the nitrogenase iron protein. Biochemistry. 43: 1787-97. PMID 14967020 DOI: 10.1021/Bi0358465 |
0.736 |
|
| 2004 |
Seefeldt LC, Dance IG, Dean DR. Substrate interactions with nitrogenase: Fe versus Mo. Biochemistry. 43: 1401-9. PMID 14769015 DOI: 10.1021/Bi036038G |
0.403 |
|
| 2003 |
Igarashi RY, Seefeldt LC. Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Critical Reviews in Biochemistry and Molecular Biology. 38: 351-84. PMID 14551236 DOI: 10.1080/10409230391036766 |
0.728 |
|
| 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 |
0.361 |
|
| 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 |
0.704 |
|
| 2003 |
Sørlie M, Chan JM, Wang H, Seefeldt LC, Parker VD. Elucidating thermodynamic parameters for electron transfer proteins using isothermal titration calorimetry: Application to the nitrogenase Fe protein Journal of Biological Inorganic Chemistry. 8: 560-566. PMID 12605257 DOI: 10.1007/S00775-003-0446-7 |
0.662 |
|
| 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 |
0.385 |
|
| 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 |
0.346 |
|
| 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 |
0.412 |
|
| 2000 |
Jang SB, Seefeldt LC, Peters JW. Insights into nucleotide signal transduction in nitrogenase: Structure of an iron protein with MgADP bound Biochemistry. 39: 14745-14752. PMID 11101289 DOI: 10.1021/Bi001705G |
0.434 |
|
| 2000 |
Sørlie M, Seefeldt LC, Parker VD. Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteins Analytical Biochemistry. 287: 118-125. PMID 11078591 DOI: 10.1006/Abio.2000.4826 |
0.354 |
|
| 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 |
0.67 |
|
| 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 |
0.358 |
|
| 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 |
0.696 |
|
| 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 |
0.362 |
|
| 2000 |
Ryle MJ, Seefeldt LC. Hydrolysis of nucleoside triphosphates other than ATP by nitrogenase. The Journal of Biological Chemistry. 275: 6214-9. PMID 10692415 DOI: 10.1074/Jbc.275.9.6214 |
0.437 |
|
| 2000 |
Jang SB, Seefeldt LC, Peters JW. Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein Biochemistry. 39: 641-648. PMID 10651628 DOI: 10.1021/Bi991694V |
0.438 |
|
| 1999 |
Chan JM, Ryle MJ, Seefeldt LC. Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complex. The Journal of Biological Chemistry. 274: 17593-8. PMID 10364195 DOI: 10.1074/Jbc.274.25.17593 |
0.686 |
|
| 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 |
0.663 |
|
| 1999 |
Lanzilotta WN, Parker VD, Seefeldt LC. Thermodynamics of nucleotide interactions with the Azotobacter vinelandii nitrogenase iron protein Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1429: 411-421. PMID 9989226 DOI: 10.1016/S0167-4838(98)00251-9 |
0.418 |
|
| 1998 |
Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science (New York, N.Y.). 282: 1853-8. PMID 9836629 DOI: 10.1126/Science.282.5395.1853 |
0.386 |
|
| 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 |
0.411 |
|
| 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 |
0.373 |
|
| 1998 |
Lanzilotta WN, Parker VD, Seefeldt LC. Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP Biochemistry. 37: 399-407. PMID 9425061 DOI: 10.1021/Bi971681M |
0.392 |
|
| 1997 |
Lanzilotta WN, Seefeldt LC. Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation Biochemistry. 36: 12976-12983. PMID 9335558 DOI: 10.1021/Bi9715371 |
0.447 |
|
| 1997 |
Liu Y, Seefeldt LC, Parker VD. Entropies of redox reactions between proteins and mediators: The temperature dependence of reversible electrode potentials in aqueous buffers Analytical Biochemistry. 250: 196-202. PMID 9245439 DOI: 10.1006/Abio.1997.2222 |
0.318 |
|
| 1997 |
Rasche ME, Seefeldt LC. Reduction of thiocyanate, cyanate, and carbon disulfide by nitrogenase: Kinetic characterization and EPR spectroscopic analysis Biochemistry. 36: 8574-8585. PMID 9214303 DOI: 10.1021/Bi970217E |
0.403 |
|
| 1997 |
Parker VD, Roddick A, Seefeldt LC, Wang H, Zheng G. Determination of rate and equilibrium constants for the reactions between electron transfer mediators and proteins by linear sweep voltammetry Analytical Biochemistry. 249: 212-218. PMID 9212873 DOI: 10.1006/Abio.1997.2176 |
0.365 |
|
| 1997 |
Parker VD, Seefeldt LC. A mediated thin-layer voltammetry method for the study of redox protein electrochemistry Analytical Biochemistry. 247: 152-157. PMID 9126385 DOI: 10.1006/Abio.1997.2049 |
0.354 |
|
| 1997 |
Lanzilotta WN, Fisher K, Seefeldt LC. Evidence for electron transfer-dependent formation of a nitrogenase iron protein-molybdenum-iron protein tight complex. The role of aspartate 391 Journal of Biological Chemistry. 272: 4157-4165. PMID 9020128 DOI: 10.1074/Jbc.272.7.4157 |
0.436 |
|
| 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 |
0.427 |
|
| 1996 |
Lanzilotta WN, Seefeldt LC. Electron transfer from the nitrogenase iron protein to the [8Fe-(7/8)S] clusters of the molybdenum-iron protein Biochemistry. 35: 16770-16776. PMID 8988014 DOI: 10.1021/Bi962286J |
0.412 |
|
| 1996 |
Ryle MJ, Seefeldt LC. The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotides. Biochemistry. 35: 15654-62. PMID 8961928 DOI: 10.1021/Bi961886F |
0.416 |
|
| 1996 |
Ryle MJ, Lanzilotta WN, Seefeldt LC. Elucidating the mechanism of nucleotide-dependent changes in the redox potential of the [4Fe-4S] cluster in nitrogenase iron protein: the role of phenylalanine 135. Biochemistry. 35: 9424-34. PMID 8755721 DOI: 10.1021/Bi9608572 |
0.426 |
|
| 1996 |
Lanzilotta WN, Fisher K, Seefeldt LC. Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein-protein complex Biochemistry. 35: 7188-7196. PMID 8679547 DOI: 10.1021/Bi9603985 |
0.442 |
|
| 1996 |
Ryle MJ, Seefeldt LC. Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineering. Biochemistry. 35: 4766-75. PMID 8664266 DOI: 10.1021/Bi960026W |
0.446 |
|
| 1996 |
Ryle MJ, Lanzilotta WN, Seefeldt LC, Scarrow RC, Jensen GM. Circular dichroism and x-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form. The Journal of Biological Chemistry. 271: 1551-7. PMID 8576152 DOI: 10.1074/Jbc.271.3.1551 |
0.41 |
|
| 1995 |
Ryle MJ, Lanzilotta WN, Mortenson LE, Watt GD, Seefeldt LC. Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes. The Journal of Biological Chemistry. 270: 13112-7. PMID 7768906 DOI: 10.1074/Jbc.270.22.13112 |
0.383 |
|
| 1995 |
Seefeldt LC, Rasche ME, Ensign SA. Carbonyl sulfide and carbon dioxide as new substrates, and carbon disulfide as a new inhibitor, of nitrogenase Biochemistry. 34: 5382-5389. PMID 7727396 DOI: 10.1021/Bi00016A009 |
0.337 |
|
| 1995 |
Lanzilotta WN, Ryle MJ, Seefeldt LC. Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129. Biochemistry. 34: 10713-23. PMID 7662655 DOI: 10.1021/Bi00034A003 |
0.449 |
|
| 1995 |
Lanzilotta WN, Holz RC, Seefeldt LC. Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Biochemistry. 34: 15646-53. PMID 7495793 DOI: 10.1021/Bi00048A007 |
0.384 |
|
| 1994 |
Seefeldt LC, Ensign SA. A continuous, spectrophotometric activity assay for nitrogenase using the reductant Titanium(III) citrate Analytical Biochemistry. 221: 379-386. PMID 7810881 DOI: 10.1006/Abio.1994.1429 |
0.35 |
|
| 1994 |
Seefeldt LC. Docking of nitrogenase iron- and molybdenum-iron proteins for electron transfer and MgATP hydrolysis: The role of arginine 140 and lysine 143 of the Azotobacter vinelandii iron protein Protein Science. 3: 2073-2081. PMID 7703853 DOI: 10.1002/Pro.5560031120 |
0.407 |
|
| 1993 |
Seefeldt LC, Mortenson LE. Increasing nitrogenase catalytic efficiency for MgATP by changing serine 16 of its Fe protein to threonine: Use of Mn2+ to show interaction of serine 16 with Mg2+ Protein Science. 2: 93-102. PMID 8443593 DOI: 10.1002/Pro.5560020110 |
0.382 |
|
| 1993 |
Mortenson L, Seefeldt L, Morgan T. The functional specificity of the amino acids of the Fe protein of nitrogenase Journal of Inorganic Biochemistry. 51: 347. DOI: 10.1016/0162-0134(93)85378-L |
0.375 |
|
| 1992 |
Hyman MR, Seefeldt LC, Vance Morgan T, Arp DJ, Mortenson LE. Kinetic and spectroscopic analysis of the inactivating effects of nitric oxide on the individual components of Azotobacter vinelandii nitrogenase Biochemistry®. 31: 2947-2955. PMID 1312859 DOI: 10.1021/Bi00126A015 |
0.413 |
|
| 1989 |
Seefeldt LC, Arp DJ. Cyanide inactivation of hydrogenase from Azotobacter vinelandii Journal of Bacteriology. 171: 3298-3303. PMID 2656648 DOI: 10.1128/Jb.171.6.3298-3303.1989 |
0.335 |
|
| 1989 |
Kovacs KL, Seefeldt LC, Tigyi G, Doyle CM, Mortenson LE, Arp DJ. Immunological relationship among hydrogenases. Journal of Bacteriology. 171: 430-5. PMID 2464579 DOI: 10.1128/Jb.171.1.430-435.1989 |
0.344 |
|
| 1988 |
Hyman MR, Seefeldt LC, Arp DJ. Aerobic, inactive forms of Azotobacter vinelandii hydrogenase: Activation kinetics and insensitivity to C2H2 inhibition Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 957: 91-96. PMID 3052594 DOI: 10.1016/0167-4838(88)90160-4 |
0.333 |
|
| 1987 |
Seefeldt LC, McCollum LC, Doyle CM, Arp DJ. Immunological and molecular evidence for a membrane-bound, dimeric hydrogenase in Rhodopseudomonas capsulata Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 914: 299-303. DOI: 10.1016/0167-4838(87)90290-1 |
0.307 |
|
| 1986 |
Seefeldt LC, Arp DJ. Purification to homogeneity of Azotobacter vinelandii hydrogenase: A nickel and iron containing αβ dimer Biochimie. 68: 25-34. PMID 3089312 DOI: 10.1016/S0300-9084(86)81064-1 |
0.357 |
|
| 1985 |
Arp DJ, McCollum LC, Seefeldt LC. Molecular and immunological comparison of membrane-bound, H2-oxidizing hydrogenases of Bradyrhizobium japonicum, Alcaligenes eutrophus, Alcaligenes latus, and Azotobacter vinelandii. Journal of Bacteriology. 163: 15-20. PMID 4008438 DOI: 10.1128/Jb.163.1.15-20.1985 |
0.341 |
|
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