Robson, R. L. & Postgate, J. R. Oxygen and hydrogen in biological nitrogen fixation. Annu. Rev. Microbiol. 34, 183–207 (1980).
Google Scholar
Robson, R. L. Characterization of an oxygen-stable nitrogenase complex isolated from Azotobacter chroococcum. Biochem. J. 181, 569–575 (1979).
Google Scholar
Shethna, Y. I., DerVartanian, D. V. & Beinert, H. Non heme (iron-sulfur) proteins of Azotobacter vinelandii. Biochem. Biophys. Res. Commun. 31, 862–868 (1968).
Google Scholar
Moshiri, F., Kim, J. W., Fu, C. L. & Maier, R. J. The FeSII protein of Azotobacter vinelandii Is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo. Mol. Microbiol. 14, 101–114 (1994).
Google Scholar
Schlesier, J., Rohde, M., Gerhardt, S. & Einsle, O. A conformational switch triggers nitrogenase protection from oxygen damage by Shethna protein II (FeSII). J. Am. Chem. Soc. 138, 239–247 (2016).
Google Scholar
Ågren, G. I., Wetterstedt, J. Å. M. & Billberger, M. F. K. Nutrient limitation on terrestrial plant growth—modeling the interaction between nitrogen and phosphorus. New Phytol. 194, 953–960 (2012).
Google Scholar
Burris, R. H. & Roberts, G. P. Biological nitrogen-fixation. Annu. Rev. Nutr. 13, 317–335 (1993).
Google Scholar
Einsle, O. & Rees, D. C. Structural enzymology of nitrogenase enzymes. Chem. Rev. 120, 4969–5004 (2020).
Google Scholar
Einsle, O. Catalysis and structure of nitrogenase. Curr. Opin. Struct. Biol. 83, 102719 (2023).
Google Scholar
Rutledge, H. L. & Tezcan, F. A. Electron transfer in nitrogenase. Chem. Rev. 120, 5158–5193 (2020).
Google Scholar
Danyal, K., Dean, D. R., Hoffman, B. M. & Seefeldt, L. C. Electron transfer within nitrogenase: evidence for a deficit-spending mechanism. Biochemistry 50, 9255–9263 (2011).
Google Scholar
Seefeldt, L. C. et al. Reduction of substrates by nitrogenases. Chem. Rev. 120, 5082–5106 (2020).
Google Scholar
Harris, D. F. et al. Mechanism of N2 reduction catalyzed by Fe-nitrogenase involves reductive elimination of H2. Biochemistry 57, 701–710 (2018).
Google Scholar
Raugei, S., Seefeldt, L. C. & Hoffman, B. M. Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N2 reduction. Proc. Natl Acad. Sci. USA 115, E10521–E10530 (2018).
Google Scholar
Trncik, C., Detemple, F. & Einsle, O. Iron-only Fe-nitrogenase underscores common catalytic principles in biological nitrogen fixation. Nat. Catal. 6, 415–424 (2023).
Google Scholar
Rohde, M., Laun, K., Zebger, I., Stripp, S. T. & Einsle, O. Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle. Sci. Adv. 7, eabg4474 (2021).
Google Scholar
Schindelin, H., Kisker, C., Sehlessman, J. L., Howard, J. B. & Rees, D. C. Structure of ADP • \({{\rm{AIF}}}_{4}^{-}\)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387, 370–376 (1997).
Google Scholar
Dixon, R. & Kahn, D. Genetic regulation of biological nitrogen fixation. Nat. Rev. Microbiol. 2, 621–631 (2004).
Google Scholar
Jacobs, D., Mitchell, D. & Watt, G. D. The concentration of cellular nitrogenase proteins in Azotobacter vinelandii whole cells as determined by activity measurements and electron paramagnetic resonance spectroscopy. Arch. Biochem. Biophys. 324, 317–324 (1995).
Google Scholar
Weiss, M. C. et al. The physiology and habitat of the last universal common ancestor. Nat. Microbiol. 1, 16116 (2016).
Google Scholar
Gallon, J. R. The oxygen sensitivity of nitrogenase—a problem for biochemists and microorganisms. Trends Biochem. Sci 6, 19–23 (1981).
Google Scholar
Zehr, J. P. Nitrogen fixation by marine cyanobacteria. Trends Microbiol. 19, 162–173 (2011).
Google Scholar
Zhang, L. & Einsle, O. Architecture of the RNF1 complex that drives biological nitrogen fixation. Nat. Chem. Biol. 20, 1078–1085 (2024).
Google Scholar
Dalton, H. & Postgate, J. R. Effect of oxygen on growth of Azotobacter chroococcum in batch and continuous cultures. J. Gen. Microbiol. 54, 463–473 (1968).
Google Scholar
Bulen, W. A. & LeComte, J. R. Nitrogenase complex and its components. Methods Enzymol. 24, 456–470 (1972).
Google Scholar
Moshiri, F., Crouse, B. R., Johnson, M. K. & Maier, R. J. The “nitrogenase-protective” FeSII protein of Azotobacter vinelandii: overexpression, characterization, and crystallization. Biochemistry 34, 12973–12982 (1995).
Google Scholar
Maier, R. J. & Moshiri, F. Role of the Azotobacter vinelandii nitrogenase-protective Shethna protein in preventing oxygen-mediated cell death. J. Bacteriol. 182, 3854–3857 (2000).
Google Scholar
Peña, C., Reyes, C., Larralde-Corona, P., Corkidi, G. & Galindo, E. Characterization of Azotobacter vinelandii aggregation in submerged culture by digital image analysis. FEMS Microbiol. Lett. 207, 173–177 (2002).
Google Scholar
Sippel, D. & Einsle, O. The structure of vanadium nitrogenase reveals an unusual bridging ligand. Nat. Chem. Biol. 13, 956–960 (2017).
Google Scholar
Kabasakal, B. V. et al. The crystal structure of Shethna protein II (FeSII) from Azotobacter vinelandii suggests a domain swap. Acta Crystallogr. D Struct. Biol. 80, 599–604 (2024).
Google Scholar
Tezcan, F. A. et al. Nitrogenase complexes: multiple docking sites for a nucleotide switch protein. Science 309, 1377–1380 (2005).
Google Scholar
Lanzilotta, W. N. & Seefeldt, L. C. 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 (1997).
Google Scholar
Veeger, C. et al. in Nitrogen Fixation Vol. 1 (eds Newton, W. E. & Orme-Johnson, W. H.) 111–137 (University Park Press, 1980).
del Campo, J. M. S. et al. Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii. Crit. Rev. Biochem. Mol. Biol. 57, 492–538 (2023).
Google Scholar
Buren, S. & Rubio, L. M. State of the art in eukaryotic nitrogenase engineering. FEMS Microbiol. Lett. 365, fnx274 (2018).
Google Scholar
Raulfs, E. C., O’Carroll, I. P., Dos Santos, P. C., Unciuleac, M. C. & Dean, D. R. In vivo iron-sulfur cluster formation. Proc. Natl Acad. Sci. USA 105, 8591–8596 (2008).
Google Scholar
Braymer, J. J. & Lill, R. Iron-sulfur cluster biogenesis and trafficking in mitochondria. J. Biol. Chem. 292, 12754–12763 (2017).
Google Scholar
Gibson, D. G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343–345 (2009).
Google Scholar
Miroux, B. & Walker, J. E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289–298 (1996).
Google Scholar
van Die, I. M., Bergmans, H. E. & Hoekstra, W. P. Transformation in Escherichia coli: studies on the role of the heat shock in induction of competence. J. Gen. Microbiol. 129, 663–670 (1983).
Google Scholar
Lipman, J. G. Experiments on the transformation and fixation of nitrogen by bacteria. Rep. NJ Agric. Exp. Stn 24, 217–285 (1903).
Google Scholar
Spatzal, T. et al. Evidence for interstitial carbon in nitrogenase FeMo cofactor. Science 334, 940 (2011).
Google Scholar
Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).
Google Scholar
Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
Google Scholar
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
Google Scholar
Punjani, A., Zhang, H. & Fleet, D. J. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214–1221 (2020).
Google Scholar
Zivanov, J., Nakane, T. & Scheres, S. H. W. Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1. IUCrJ 7, 253–267 (2020).
Google Scholar
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).
Google Scholar
Varadi, M. et al. AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res. 50, D439–D444 (2022).
Google Scholar
Goddard, T. D. et al. UCSF ChimeraX: meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018).
Google Scholar
Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126–2132 (2004).
Google Scholar
Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr. D Struct. Biol. 75, 861–877 (2019).
Google Scholar
Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12–21 (2010).
Google Scholar
Vonrhein, C. et al. Data processing and analysis with the autoPROC toolbox. Acta Crystallogr. D Biol. Crystallogr. 67, 293–302 (2011).
Google Scholar
Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D Biol. Crystallogr. 69, 1204–1214 (2013).
Google Scholar
Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235–242 (2011).
Google Scholar
Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022–1025 (1997).
Google Scholar
Vagin, A. A. et al. REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr. D Biol. Crystallogr. 60, 2184–2195 (2004).
Google Scholar
