title: The prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic.
abstract: Over 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.
authors: Aix Marseille Université, Unité de Bioénergétique et Ingénierie des Protéines, Marseille Cedex 20, France.
authors: Stéphane
authors: S
authors: Grimaldi
authors: Barbara
authors: B
authors: Schoepp-Cothenet
authors: Pierre
authors: P
authors: Ceccaldi
authors: Bruno
authors: B
authors: Guigliarelli
authors: Axel
authors: A
authors: Magalon
mesh_terms: D002384:Catalysis; D004734:Energy Metabolism; D004798:Enzymes / Q000378:metabolism*; D008024:Ligands
chemical_list: D004798:Enzymes; D008024:Ligands
keywords: Bioenergetic; Electron transfer; Iron–sulfur; Molybdenum; Prokaryote; Quinone