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.
Author details: | Kenichi Yokoyama, Silke LeimkühlerORCiDGND |
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DOI: | https://doi.org/10.1016/j.bbamcr.2014.09.021 |
ISSN: | 0167-4889 |
ISSN: | 0006-3002 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/25268953 |
Title of parent work (English): | Biochimica et biophysica acta : Molecular cell research |
Publisher: | Elsevier |
Place of publishing: | Amsterdam |
Publication type: | Review |
Language: | English |
Year of first publication: | 2015 |
Publication year: | 2015 |
Release date: | 2017/03/27 |
Tag: | L-Cysteine desulfurase; Molybdenum cofactor; Molybdenum-iron-iron-sulfur cluster; Sulfur transfer; tRNA |
Volume: | 1853 |
Issue: | 6 |
Number of pages: | 15 |
First page: | 1335 |
Last Page: | 1349 |
Funding institution: | Deutsche Forschungsgemeinschaft [LE1171] |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
Peer review: | Referiert |