The mechanism for nitrogenase including all steps-Reference-Cited by-同舟云学术

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The mechanism for nitrogenase including all steps

Published:2019 Issue:28 Volume:21 Page:15747-15759
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Siegbahn Per E. M.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Organic Chemistry

2. Arrhenius Laboratory

3. Stockholm University

4. Stockholm

5. Sweden

Abstract

Nitrogen in the air is turned into biologically useful ammonia by the nitrogenase enzyme. The leading member of this group has a cofactor with one molybdenum and seven irons linked together by sulfurs. The structure that binds N₂ has a triply protonated carbide and a rotated homocitrate. Both these structural changes are necessary for the activation.

Funder

Vetenskapsrådet

Knut och Alice Wallenbergs Stiftelse

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP02073J

Reference46 articles.

1. Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein

2. Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

3. R. N. F. Thorneley and D. J.Lowe , Molybdenum Enzymes , ed. T. Spiro , Wiley , N.Y. , 1985 , p. 221

4. Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage

5. Nitrogenase: A Draft Mechanism

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