@article{f42061daffe44e26a0ff721bb8367305,
title = "Control of electron transfer in nitrogenase",
abstract = " The bacterial enzyme nitrogenase achieves the reduction of dinitrogen (N 2 ) to ammonia (NH 3 ) utilizing electrons, protons, and energy from the hydrolysis of ATP. Building on earlier foundational knowledge, recent studies provide molecular-level details on how the energy of ATP hydrolysis is utilized, the sequencing of multiple electron transfer events, and the nature of energy transduction across this large protein complex. Here, we review the state of knowledge about energy transduction in nitrogenase. ",
author = "Seefeldt, {Lance C.} and Peters, {John W.} and Beratan, {David N.} and Brian Bothner and Minteer, {Shelley D.} and Simone Raugei and Hoffman, {Brian M.}",
note = "Funding Information: This work was supported as part of the Biological Electron Transfer and Catalysis (BETCy) Energy Frontier Research Center (EFRC) funded by the United States Department of Energy (U.S. DOE), Office of Science, Basic Energy Sciences (DE-SC0012518). S.R. was supported by the U.S. DOE, Office of Science, Basic Energy Sciences, Division of Chemical Sciences, Geosciences, and Bio-Sciences (DE-AC05-76RL01830/FWP6647). B.M.H. was supported by the National Institutes of Health (GM111097). J.W.P. and L.C.S. were supported by the National Science Foundation (MCB 1330807). Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",
year = "2018",
month = dec,
doi = "10.1016/j.cbpa.2018.08.011",
language = "English",
volume = "47",
pages = "54--59",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",
publisher = "Elsevier Limited",
}