JBIC Journal of Biological Inorganic Chemistry

, Volume 6, Issue 3, pp 209–226

Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role

  • Jennifer Cheek
  • Joan B. Broderick
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DOI: 10.1007/s007750100210

Cite this article as:
Cheek, J. & Broderick, J. J. Biol. Inorg. Chem. (2001) 6: 209. doi:10.1007/s007750100210

Abstract.

Iron-sulfur clusters are widespread in biological systems and participate in a broad range of functions. These functions include electron transport, mediation of redox as well as non-redox catalysis, and regulation of gene expression. A new role for iron-sulfur clusters has emerged in recent years as a number of enzymes have been identified that utilize Fe-S clusters and S-adenosylmethionine (AdoMet) to initiate radical catalysis. This Fe-S cluster-mediated radical catalysis includes the generation of stable protein-centered radicals as well as generation of substrate radical intermediates, with evidence suggesting a common mechanism involving an intermediate adenosyl radical. Although the mechanism of generation of the adenosyl radical intermediate is currently not well understood, it likely represents novel chemistry for iron-sulfur clusters. The purpose of this review is to present the current state of knowledge of this newly emerging group of Fe-S/AdoMet enzymes.

Iron-sulfur cluster Radical generation Adenosylmethionine Protein radicals 

Copyright information

© SBIC 2001

Authors and Affiliations

  • Jennifer Cheek
    • 1
  • Joan B. Broderick
    • 1
  1. 1.Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA

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