Structural enzymology of nitrogenase enzymes

O Einsle, DC Rees - Chemical reviews, 2020 - ACS Publications
The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography
involving two component proteins, MgATP and reductant. At center stage of this process …

Near ambient N2 fixation on solid electrodes versus enzymes and homogeneous catalysts

O Westhead, J Barrio, A Bagger, JW Murray… - Nature Reviews …, 2023 - nature.com
Abstract The Mo/Fe nitrogenase enzyme is unique in its ability to efficiently reduce
dinitrogen to ammonia at atmospheric pressures and room temperature. Should an artificial …

Reactivity, mechanism, and assembly of the alternative nitrogenases

AJ Jasniewski, CC Lee, MW Ribbe, Y Hu - Chemical reviews, 2020 - ACS Publications
Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the
cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated …

Structures of the nitrogenase complex prepared under catalytic turnover conditions

HL Rutledge, BD Cook, HPM Nguyen, MA Herzik Jr… - Science, 2022 - science.org
The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the
multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research …

[HTML][HTML] Tunnel engineering of gas-converting enzymes for inhibitor retardation and substrate acceleration

SM Kim, SH Kang, BW Jeon, YH Kim - Bioresource Technology, 2024 - Elsevier
Carbon monoxide dehydrogenase (CODH), formate dehydrogenase (FDH), hydrogenase
(H2ase), and nitrogenase (N2ase) are crucial enzymatic catalysts that facilitate the …

Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system

SD Threatt, DC Rees - FEBS letters, 2023 - Wiley Online Library
Nitrogenase is the sole enzyme responsible for the ATP‐dependent conversion of
atmospheric dinitrogen into the bioavailable form of ammonia (NH3), making this protein …

Small-molecule tunnels in metalloenzymes viewed as extensions of the active site

R Banerjee, JD Lipscomb - Accounts of chemical research, 2021 - ACS Publications
Conspectus Rigorous substrate selectivity is a hallmark of enzyme catalysis. This selectivity
is generally ascribed to a thermodynamically favorable process of substrate binding to the …

Escapement mechanisms and the conversion of disequilibria; the engines of creation

E Branscomb, T Biancalani, N Goldenfeld, M Russell - Physics Reports, 2017 - Elsevier
Virtually every interesting natural phenomenon, not least life itself, entails physical systems
being forced to flow thermodynamically up-hill, away from equilibrium rather than towards it …

Structural consequences of turnover-induced homocitrate loss in nitrogenase

RA Warmack, AO Maggiolo, A Orta, BB Wenke… - Nature …, 2023 - nature.com
Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the
process of biological nitrogen fixation that is essential for sustaining life. The active site …

Characterization of the Earliest Intermediate of Fe-N2 Protonation: CW and Pulse EPR Detection of an Fe-NNH Species and Its Evolution to Fe-NNH2+

MA Nesbit, PH Oyala, JC Peters - Journal of the American …, 2019 - ACS Publications
Iron diazenido species (Fe (NNH)) have been proposed as the earliest intermediates of
catalytic N2-to-NH3 conversion (N2RR) mediated by synthetic iron complexes and relatedly …