Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role
- PMID: 11315557
- DOI: 10.1007/s007750100210
Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role
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.
Similar articles
-
Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme.J Am Chem Soc. 2002 Mar 27;124(12):3143-51. doi: 10.1021/ja012034s. J Am Chem Soc. 2002. PMID: 11902903
-
Pyruvate formate-lyase activating enzyme: elucidation of a novel mechanism for glycyl radical formation.Arch Biochem Biophys. 2005 Jan 1;433(1):288-96. doi: 10.1016/j.abb.2004.09.028. Arch Biochem Biophys. 2005. PMID: 15581584 Review.
-
Adenosylmethionine as a source of 5'-deoxyadenosyl radicals.Curr Opin Chem Biol. 2001 Oct;5(5):506-11. doi: 10.1016/s1367-5931(00)00237-4. Curr Opin Chem Biol. 2001. PMID: 11578923 Review.
-
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study.J Am Chem Soc. 2002 Feb 13;124(6):912-3. doi: 10.1021/ja017562i. J Am Chem Soc. 2002. PMID: 11829592
-
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.Nat Chem Biol. 2013 May;9(5):333-8. doi: 10.1038/nchembio.1229. Epub 2013 Mar 31. Nat Chem Biol. 2013. PMID: 23542644 Free PMC article.
Cited by
-
An investigation of the catalytic mechanism of S-adenosylmethionine synthetase by QM/MM calculations.Arch Biochem Biophys. 2009 Dec;492(1-2):82-92. doi: 10.1016/j.abb.2009.08.010. Epub 2009 Aug 20. Arch Biochem Biophys. 2009. PMID: 19699176 Free PMC article.
-
Mechanistic Studies of Radical SAM Enzymes: Pyruvate Formate-Lyase Activating Enzyme and Lysine 2,3-Aminomutase Case Studies.Methods Enzymol. 2018;606:269-318. doi: 10.1016/bs.mie.2018.04.013. Epub 2018 Jul 7. Methods Enzymol. 2018. PMID: 30097096 Free PMC article.
-
Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.EMBO J. 2003 Dec 1;22(23):6214-24. doi: 10.1093/emboj/cdg598. EMBO J. 2003. PMID: 14633981 Free PMC article.
-
Radical SAM enzymes: Nature's choice for radical reactions.FEBS Lett. 2023 Jan;597(1):92-101. doi: 10.1002/1873-3468.14519. Epub 2022 Oct 27. FEBS Lett. 2023. PMID: 36251330 Free PMC article. Review.
-
Essentiality of the Escherichia coli YgfZ Protein for the In Vivo Thiomethylation of Ribosomal Protein S12 by the RimO Enzyme.Int J Mol Sci. 2023 Mar 1;24(5):4728. doi: 10.3390/ijms24054728. Int J Mol Sci. 2023. PMID: 36902159 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous