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 SiedowA 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 BiomembranesISSN
0145-479XExternal DOI
Issue
4Volume
27Page range
367-377Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
Categories
No categories selectedKeywords
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC