University of Sussex
Browse

File(s) not publicly available

Strucute-Funtion-Relationships of the Alternative Oxidase of Plant-Mitochondria - A Model of the Active-Site

journal contribution
posted on 2023-06-08, 00:43 authored by Anthony Moore, Ann L Umbach, James N Siedow
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.

History

Publication status

  • Published

Journal

Journal of Bioenergetics and Biomembranes

ISSN

0145-479X

Issue

4

Volume

27

Page range

367-377

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC