Radical AdoMet enzymes in complex metal cluster biosynthesis

Benjamin R. Duffus, Trinity L. Hamilton, Eric M. Shepard, Eric S. Boyd, John W. Peters, Joan B. Broderick

Research output: Contribution to journalReview articlepeer-review

21 Scopus citations

Abstract

Radical S-adenosylmethionine (AdoMet) enzymes comprise a large superfamily of proteins that engage in a diverse series of biochemical transformations through generation of the highly reactive 5′-deoxyadenosyl radical intermediate. Recent advances into the biosynthesis of unique iron-sulfur (FeS)-containing cofactors such as the H-cluster in [FeFe]-hydrogenase, the FeMo-co in nitrogenase, as well as the iron-guanylylpyridinol (FeGP) cofactor in [Fe]-hydrogenase have implicated new roles for radical AdoMet enzymes in the biosynthesis of complex inorganic cofactors. Radical AdoMet enzymes in conjunction with scaffold proteins engage in modifying ubiquitous FeS precursors into unique clusters, through novel amino acid decomposition and sulfur insertion reactions. The ability of radical AdoMet enzymes to modify common metal centers to unusual metal cofactors may provide important clues into the stepwise evolution of these and other complex bioinorganic catalysts. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.

Original languageEnglish (US)
Pages (from-to)1254-1263
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1824
Issue number11
DOIs
StatePublished - Nov 2012

Bibliographical note

Funding Information:
The authors are grateful for support by the NASA Astrobiology Institute (NAI)-Funded Astrobiology Biogeocatalysis Research Center NNA08C-N85A (J.B.B. and J.W.P.), the Department of Energy Office of Basic Energy Sciences DE-FG02-10ER16194 (J.B.B. and J.W.P.), AFOSR Multidisciplinary University Research Initiative Award FA9550-05-01-0365 (J.W.P.), and NSF ETBC grant 1024614 (E.S.B.). T.L.H. was supported by an NSF-Integrated Graduate Educational Research and Training fellowship grant. Aspects of this research were carried out at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences.

Keywords

  • Biosynthesis
  • Hydrogenase
  • Iron-sulfur cluster
  • Nitrogenase
  • Radical S-adenosylmethionine enzyme
  • Scaffold protein

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