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The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria

  • The biosynthesis of the molybdenum cofactor (Moco) has been intensively studied, in addition to its insertion into molybdoenzymes. In particular, a link between the assembly of molybdoenzymes and the biosynthesis of FeS clusters has been identified in the recent years: 1) the synthesis of the first intermediate in Moco biosynthesis requires an FeS-cluster containing protein, 2) the sulfurtransferase for the dithiolene group in Moco is also involved in the synthesis of FeS clusters, thiamin and thiolated tRNAs, 3) the addition of a sulfido-ligand to the molybdenum atom in the active site additionally involves a sulfurtransferase, and 4) most molybdoenzymes in bacteria require FeS clusters as redox active cofactors. In this review we will focus on the biosynthesis of the molybdenum cofactor in bacteria, its modification and insertion into molybdoenzymes, with an emphasis to its link to FeS cluster biosynthesis and sulfur transfer. (C) 2014 Elsevier B.V. All rights reserved.

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Author:Kenichi Yokoyama, Silke Leimkühler
ISSN:0167-4889 (print)
ISSN:0006-3002 (online)
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=25268953
Parent Title (English):Biochimica et biophysica acta : Molecular cell research
Place of publication:Amsterdam
Document Type:Review
Year of first Publication:2015
Year of Completion:2015
Release Date:2017/03/27
Tag:L-Cysteine desulfurase; Molybdenum cofactor; Molybdenum-iron-iron-sulfur cluster; Sulfur transfer; tRNA
First Page:1335
Last Page:1349
Funder:Deutsche Forschungsgemeinschaft [LE1171]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert