2016
DOI: 10.1002/ijch.201600020
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Electron Transfer Reactions in Biological Nitrogen Fixation

Abstract: In this review, we summarize our recent efforts toward understanding electron transfer (ET) processes in nitrogenase, the only enzyme capable of reducing dinitrogen to ammonia. We discuss new structural and biochemical perspectives on the role of ATP‐dependent interactions between the two components of nitrogenase, Fe‐protein (FeP) and MoFe‐protein (MoFeP), and how these interactions may regulate interprotein ET and catalysis. We also discuss the implications of our work on FeP‐ and ATP‐independent, photoredox… Show more

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Cited by 12 publications
(14 citation statements)
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“…As shown in Equation 2, each enzymatic turnover reaction by nitrogenase is an 8-e − process. These electrons are delivered one at a time to MoFeP by FeP, with two ATP molecules consumed by FeP for of each electron transferred [33, 57]. FeP is the only known biological agent that can reduce MoFeP and activate it for catalysis.…”
Section: Introductionmentioning
confidence: 99%
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“…As shown in Equation 2, each enzymatic turnover reaction by nitrogenase is an 8-e − process. These electrons are delivered one at a time to MoFeP by FeP, with two ATP molecules consumed by FeP for of each electron transferred [33, 57]. FeP is the only known biological agent that can reduce MoFeP and activate it for catalysis.…”
Section: Introductionmentioning
confidence: 99%
“…These observations underscore the importance of specific ATP-dependent interactions between these two proteins and implies the presence of conformationally gated redox events (see sections 1.2 and 1.3). Electrons donated by FeP are first received by the P-cluster and then relayed to FeMoco, which reduces substrates in a stepwise fashion (Figure 2) [29, 33, 36, 57, 68].…”
Section: Introductionmentioning
confidence: 99%
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