The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.
Journal Article (Journal Article;Review)
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.
Full Text
Duke Authors
Cited Authors
- Yokoyama, K; Leimkühler, S
Published Date
- June 2015
Published In
Volume / Issue
- 1853 / 6
Start / End Page
- 1335 - 1349
PubMed ID
- 25268953
Pubmed Central ID
- PMC4834969
International Standard Serial Number (ISSN)
- 0006-3002
Digital Object Identifier (DOI)
- 10.1016/j.bbamcr.2014.09.021
Language
- eng
Conference Location
- Netherlands