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Title: Radical S-Adenosyl-L-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors

Abstract

Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. Furthermore, the FeMo cofactor of nitrogenase has a MoFe 7S 9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligands at a mononuclear iron site. Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assembly of all three of these diverse cofactors. Here, in this minireview, we present and discuss the current state of knowledge of the radical S-adenosylmethionine enzymes required for synthesis of these remarkable metal cofactors.

Authors:
 [1];  [1];  [1];  [1]
  1. Montana State Univ., Bozeman, MT (United States). Dept. of Chemistry and Biochemistry
Publication Date:
Research Org.:
Montana State Univ., Bozeman, MT (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1356203
Grant/Contract Number:  
SC0005404
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Biological Chemistry
Additional Journal Information:
Journal Volume: 290; Journal Issue: 7; Journal ID: ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular Biology
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; Hydrogenase; Iron-Sulfur Protein; Nitrogenase; Radical; S-Adenosylmethionine (SAM)

Citation Formats

Byer, Amanda S., Shepard, Eric M., Peters, John W., and Broderick, Joan B. Radical S-Adenosyl-L-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors. United States: N. p., 2014. Web. doi:10.1074/jbc.R114.578161.
Byer, Amanda S., Shepard, Eric M., Peters, John W., & Broderick, Joan B. Radical S-Adenosyl-L-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors. United States. doi:10.1074/jbc.R114.578161.
Byer, Amanda S., Shepard, Eric M., Peters, John W., and Broderick, Joan B. Thu . "Radical S-Adenosyl-L-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors". United States. doi:10.1074/jbc.R114.578161. https://www.osti.gov/servlets/purl/1356203.
@article{osti_1356203,
title = {Radical S-Adenosyl-L-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors},
author = {Byer, Amanda S. and Shepard, Eric M. and Peters, John W. and Broderick, Joan B.},
abstractNote = {Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. Furthermore, the FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligands at a mononuclear iron site. Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assembly of all three of these diverse cofactors. Here, in this minireview, we present and discuss the current state of knowledge of the radical S-adenosylmethionine enzymes required for synthesis of these remarkable metal cofactors.},
doi = {10.1074/jbc.R114.578161},
journal = {Journal of Biological Chemistry},
number = 7,
volume = 290,
place = {United States},
year = {2014},
month = {12}
}

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