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

Published

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

  • 25268953

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/j.bbamcr.2014.09.021

Language

  • eng

Conference Location

  • Netherlands