Nitrogenase Mechanism: Electron and Proton Accumulation and N2 Reduction

Lance C. Seefeldt, Dennis R. Dean, Brian M. Hoffman

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Nitrogenase is the enzyme responsible for all biological nitrogen fixation, catalyzing the reduction of dinitrogen (N2) to ammonia (NH3). The best studied and most widespread nitrogenase contains a Mo cofactor called FeMo-co. Here, we focus on three aspects of nitrogenase catalysis. (i) We review the current state of knowledge about how electrons are delivered and accumulated to achieve the challenging reduction of N2. This includes a detailed view of the roles of ATP hydrolysis in the reaction. (ii) A brief description is presented of a recent study of alternative substrates that supports the proposal that nitrogenase carries out nitrogen fixation through an "Alternating Pathway". (iii) Building on recent insights into how electrons and protons are accumulated on FeMo-co, we review the studies that establish the obligatory evolution of an H2 for each N2 reduced. The resulting reductive-elimination/oxidative addition model for how FeMo-co is activated for N2 binding and reduction is described.

Original languageEnglish (US)
Title of host publicationMolybdenum and Tungsten Enzymes
Subtitle of host publicationBiochemistry
EditorsC. David Garner, Russ Hille, Carola Schulzke, Martin L. Kirk
PublisherRoyal Society of Chemistry
Pages274-296
Number of pages23
Edition5
DOIs
StatePublished - 2017

Publication series

NameRSC Metallobiology
Number5
Volume2017-January
ISSN (Print)2045-547X

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (miscellaneous)

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