The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necator

Sheron Hakopian; Dimitri Niks; Russ Hille

doi:10.1016/j.jinorgbio.2022.111788

The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necator

J Inorg Biochem. 2022 Jun:231:111788. doi: 10.1016/j.jinorgbio.2022.111788. Epub 2022 Mar 10.

Authors

Sheron Hakopian¹, Dimitri Niks¹, Russ Hille²

Affiliations

¹ Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA.
² Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA. Electronic address: russ.hille@ucr.edu.

PMID: 35313132
DOI: 10.1016/j.jinorgbio.2022.111788

Abstract

The nature of air-inactivation of the formate dehydrogenase FdsDABG from Cupriavidus necator has been investigated. It is found that superoxide, generated in the reaction of reduced enzyme with oxygen, is responsible for the loss of activity and that superoxide dismutase protects the enzyme from air-inactivation. Inhibition appears to be due to the reaction of superoxide with the catalytically essential MoS group of the enzyme's molybdenum center in such a way that generates sulfite. SYNOPSIS: Superoxide generated in the reaction of reduced formate dehydrogenase FdsDABG from Cupriavidus necator with O₂ is found to be responsible for the loss of activity. Catalytic amounts of superoxide dismutase are found to protect FdsDABG just as well as more generally used stabilizing inhibitors such as nitrate.

Keywords: FdsDABG; Formate dehydrogenase; Steady-state kinetics; Superoxide; Superoxide dismutase; Xanthine oxidase.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Catalysis
Cupriavidus necator*
Formate Dehydrogenases*
Superoxide Dismutase
Superoxides

Substances

Superoxides
Superoxide Dismutase
Formate Dehydrogenases