Flavoenzymes reduce vanadium(V) and molecular oxygen and generate hydroxyl radical

Xianglin Shi, N. S. Dalal

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

ESR spectroscopic evidence is presented for the formation of vanadium(IV) in the reduction of vanadium(V) by three typical, NADPH-dependent, flavoenzymes: glutathione reductase, lipoyl dehydrogenase, and ferredoxin-NADP+ oxidoreductase. The vanadium(V)-reduction mechanism appears to be an enzymatic one-electron reduction process. Addition of superoxide dismutase (SOD) showed that the generation of vanadium(IV) does not involve the superoxide (O2-) radical significantly. Measurements under anaerobic atmosphere showed, however, that the enzymes-vanadium-NADPH mixture can cause the reduction of molecular oxygen to generate H2O2. The H2O2 and vanadium(IV) thus formed react to generate hydroxyl (· OH) radical. The · OH formation is inhibited strongly by catalase and to a lesser degree by SOD, but it is enhanced by exogenous H2O2, suggesting the occurrence of a Fenton-like reaction. The inhibition of vanadium(IV) formation by N-ethylmaleimide indicates that the SH group on the flavoenzyme's cystine residueplays an important role in the enzyme's vanadium(V) reductase function. These results thus reveal a new property of the above-mentioned, NADPH-dependent flavoenzymes-their function as vanadium(V) reductases, as well as that as generators of · OH radical in the vanadium(V) reduction mechanism.

Original languageEnglish
Pages (from-to)355-361
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume289
Issue number2
DOIs
StatePublished - Sep 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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