Interaction of iron-sulfur flavoprotein with oxygen and hydrogen peroxide

Biochimica Et Biophysica Acta
F Cruz, James G Ferry

Abstract

The dimeric iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila contains one 4Fe-4S center and one FMN per monomer, and is the prototype of a family widely distributed among strictly anaerobic prokaryotes. Although Isf is able to oxidize ferredoxin, the physiological electron acceptor is unknown; thus, the ability of Isf to reduce O2 and H2O2 was investigated. The product of O2 or H2O2 reduction by Isf was determined to be water. The kinetic parameters of the oxidative half-reactions with O2 and H2O2 as electron acceptors were consistent with a role for Isf in combating oxidative stress. Isf depleted of the 4Fe-4S cluster was unable to oxidize ferredoxin and reduce the FMN cofactor, supporting a role for the cluster in transfer of electrons from ferredoxin to the cofactor. The implications of these properties on the possible function and mechanism of Isf are discussed.

Citations

Nov 8, 2011·Antioxidants & Redox Signaling·R Luise Krauth-Siegel, Alejandro E Leroux
Apr 2, 2008·Annals of the New York Academy of Sciences·James G Ferry, Daniel J Lessner
Feb 10, 2019·Applied and Environmental Microbiology·Tianning PuZhijun Wang
Sep 5, 2019·Frontiers in Microbiology·Sarah NaiyerSudha Bhattacharya

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