Superoxidized states of Escherichia coli sulfite reductase heme protein subunit.

Published

Journal Article

The oxidized forms of resting and sulfite-complexed Escherichia coli sulfite reductase heme protein subunit react with near-stoichiometric amounts of porphyrexide to produce what is best characterized as a ferrisiroheme pi cation radical. Addition of either sodium ascorbate or NADPH completely regenerates the parent form. Implications of these findings with respect to mechanisms of metal-radical J coupling and catalysis are discussed.

Full Text

Duke Authors

Cited Authors

  • Young, LJ; Siegel, LM

Published Date

  • August 9, 1988

Published In

Volume / Issue

  • 27 / 16

Start / End Page

  • 5984 - 5990

PubMed ID

  • 3056517

Pubmed Central ID

  • 3056517

International Standard Serial Number (ISSN)

  • 0006-2960

Language

  • eng

Conference Location

  • United States