Interaction of iron-sulfur flavoprotein with oxygen and hydrogen peroxide

Francisco Cruz, James Gregory Ferry

Research output: Contribution to journalArticle

16 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)858-864
Number of pages7
JournalBiochimica et Biophysica Acta - General Subjects
Volume1760
Issue number6
DOIs
StatePublished - Jun 1 2006

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Flavoproteins
Sulfur
Hydrogen Peroxide
Iron
Oxygen
Ferredoxins
Flavin Mononucleotide
Electrons
Oxidative stress
Kinetic parameters
Oxidative Stress
Monomers
Water

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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Interaction of iron-sulfur flavoprotein with oxygen and hydrogen peroxide. / Cruz, Francisco; Ferry, James Gregory.

In: Biochimica et Biophysica Acta - General Subjects, Vol. 1760, No. 6, 01.06.2006, p. 858-864.

Research output: Contribution to journalArticle

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