AcsF catalyzes the ATP-dependent insertion of Nickel into the Ni, Ni-[4Fe4S] cluster of Acetyl-CoA synthase
Journal article
Publication Details
Author list: Gregg C.M., Goetzl S., Jeoung J.H., Dobbek H.
Journal: Journal of Biological Chemistry
Publication year: 2016
Volume number: 291
Issue number: 35
Pages: 18129-18138
Publisher: American Society for Biochemistry and Molecular Biology Inc.
URL: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84984788318&origin=inward
Languages: English-Great Britain
Abstract
Acetyl-CoA synthase (ACS) catalyzes the reversible condensation of CO, CoA, and a methyl-cation to form acetyl-CoA at a unique Ni,Ni-[4Fe4S] cluster (the A-cluster). However, it was unknown which proteins support the assembly of the A-cluster. We analyzed the product of a gene from the cluster containing the ACS gene, cooC2 from Carboxydothermus hydrogeno for mans, named AcsFCh, and showed that it acts as a maturation factor of ACS. AcsFCh and inactive ACS form a stable 2:1 complex that binds two nickel ions with higher affinity than the individual components. The nickel-bound ACS-AcsFCh complex remains inactive until MgATP is added, thereby converting inactive to active ACS. AcsFCh is a Min D-type ATPase and belongs to the CooC protein family, which can be divided into homologous subgroups. We propose that proteins of one subgroup are responsible for assembling the Ni,Ni-[4Fe4S] cluster of ACS, whereas proteins of a second subgroup mature the [Ni4Fe4S] cluster of carbon monoxide dehydrogenases.
