Superoxidized states of Escherichia coli sulfite reductase heme protein subunit.
Journal Article (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
International Standard Serial Number (ISSN)
- 0006-2960
Digital Object Identifier (DOI)
- 10.1021/bi00416a023
Language
- eng
Conference Location
- United States