Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site.

Journal Article (Review)

A major characteristic of plant mitochondria is the presence of a cyanide-insensitive alternative oxidase which catalyzes the reduction of oxygen to water. Current information on the properties of the oxidase is reviewed. Conserved amino acid motifs have been identified which suggest the presence of a hydroxo-bridged di-iron center in the active site of the alternative oxidase. On the basis of sequence comparison with other di-iron center proteins, a structural model for the active site of the alternative oxidase has been developed that has strong similarity to that of methane monoxygenase. Evidence is presented to suggest that the alternative oxidase of plant mitochondria is the newest member of the class II group of di-iron center proteins.

Full Text

Duke Authors

Cited Authors

  • Moore, AL; Umbach, AL; Siedow, JN

Published Date

  • August 1995

Published In

Volume / Issue

  • 27 / 4

Start / End Page

  • 367 - 377

PubMed ID

  • 8595972

International Standard Serial Number (ISSN)

  • 0145-479X

Language

  • eng

Conference Location

  • United States