The reaction of 8-mercaptoflavins and flavoproteins with sulfite. Evidence for the role of an active site arginine in D-amino acid oxidase.

P. F. Fitzpatrick, V. Massey

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23 Scopus citations

Abstract

This work presents strong evidence that the role of the active site arginine in D-amino acid oxidase is to act as a positively charged group interacting with the flavin N(1)-C(2) = 0 locus. Modification with cyclohexanedione, which has been shown previously to modify specifically an active site arginine in D-amino acid oxidase (Ferti, C., Curti, B., Simonetta, M. P., Ronchi, S., Galliano, M., and Minchiotti, L. (1981) Eur. J. Biochem. 119, 553-557) destroys the ability of D-amino acid oxidase to stabilize the benzoquinoid type spectrum of 8-mercapto-FAD and destroys the ability to form a flavin N-5 adduct with sulfite. Both of these properties have been attributed to the presence of such a group. The active site lysine, histidine, and tyrosine have been ruled out as possibilities for such a group. In addition, the reactivity of flavoproteins containing 8-mercaptoflavin with sulfite has been examined and falls into the same two general classes as the reactivity of the native flavoproteins: oxidases form N-5 adducts while all of the other 8-mercaptoflavoproteins examined do not, forming instead the 8-sulfonate flavin.

Original languageEnglish (US)
Pages (from-to)9700-9705
Number of pages6
JournalJournal of Biological Chemistry
Volume258
Issue number16
StatePublished - Aug 25 1983

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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