NDLI: The controlled relay of multiple protons required at the active site of nitrogenase

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The controlled relay of multiple protons required at the active site of nitrogenase

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The controlled relay of multiple protons required at the active site of nitrogenase

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dance, Ian
Description	Author Affiliation: Dance I ( School of Chemistry, University of New South Wales, Sydney 2052, Australia. i.dance@unsw.edu.au)
Abstract	The enzyme nitrogenase, when reducing natural and unnatural substrates, requires large numbers of protons per chemical catalytic cycle. The active face of the catalytic site (the FeMo-cofactor, FeMo-co) is situated in a protein domain which is largely hydrophobic and anhydrous, and incapable of serial provision of multiple protons. Through detailed analysis of the high quality protein crystal structures available the characteristics of a chain of water molecules leading from the protein surface to a key sulfur atom (S3B) of FeMo-co are described. The first half of the water chain from the surface inwards is branched, slightly variable, and able to accommodate exogenous small molecules: this is dubbed the proton bay. The second half, from the proton bay to S3B, is comprised of a single chain of eight hydrogen bonded water molecules. This section is strictly conserved, and is intimately involved in hydrogen bonds with homocitrate, an essential component that chelates Mo. This is the proton wire, and a detailed Grotthuss mechanism for serial translocation of protons through this proton wire to S3B is proposed. This controlled serial proton relay from the protein surface to S3B is an essential component of the intramolecular hydrogenation paradigm for the complete chemical mechanisms of nitrogenase. Each proton reaching S3B, instigated by electron transfer to FeMo-co, becomes a hydrogen atom that migrates to other components of the active face of FeMo-co and to bound substrates and intermediates, allowing subsequent multiple proton transfers along the proton wire. Experiments to test the proposed mechanism of proton supply are suggested. The water chain in nitrogenase is comparable with the purported proton pumping pathway of cytochrome c oxidase.
ISSN	14779226
Issue Number	25
Volume Number	41
e-ISSN	13645447
Journal	Dalton Trans.
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2012-07-07
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Nitrogenase Chemistry Protons Azotobacter Enzymology Catalytic Domain Hydrogen Bonding Iron Models, Molecular Molybdenum Metabolism Proteins Water Journal Article Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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