Article thumbnail

The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic

By Stéphane Grimaldi, Barbara Schoepp-Cothenet, Pierre Ceccaldi, Bruno Guigliarelli and Axel Magalon

Abstract

AbstractOver the past two decades, prominent importance of molybdenum-containing enzymes in prokaryotes has been put forward by studies originating from different fields. Proteomic or bioinformatic studies underpinned that the list of molybdenum-containing enzymes is far from being complete with to date, more than fifty different enzymes involved in the biogeochemical nitrogen, carbon and sulfur cycles. In particular, the vast majority of prokaryotic molybdenum-containing enzymes belong to the so-called dimethylsulfoxide reductase family. Despite its extraordinary diversity, this family is characterized by the presence of a Mo/W-bis(pyranopterin guanosine dinucleotide) cofactor at the active site. This review highlights what has been learned about the properties of the catalytic site, the modular variation of the structural organization of these enzymes, and their interplay with the isoprenoid quinones. In the last part, this review provides an integrated view of how these enzymes contribute to the bioenergetics of prokaryotes. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems

Publisher: Elsevier B.V.
Year: 2013
DOI identifier: 10.1016/j.bbabio.2013.01.011
OAI identifier:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • https://s3.amazonaws.com/prod-... (external link)
  • https://s3-eu-west-1.amazonaws... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.