The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center

FEBS Letters

Umbach, Ann L.²  Moore, Anthony L.¹  Siedow, James N.² 

[1] Biochemistry Department, University of Sussex, Falmer, Brighton BN1 9QG, UK;DCMB/Botany, Box 91000, Duke University, Durham, NC 27708-1000, USA

关键词: Cyanide-resistant oxidase;    Binuclear iron protein;    Plant mitochondria;    Active site model;   

DOI  :  10.1016/0014-5793(95)00196-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cyanide-resistant, alternative oxidase of plant mitochondria catalyzes the four-electron reduction of oxygen to water, but the nature of the catalytic center associated with this oxidase has yet to be elucidated. We have identified conserved amino acids, including two copies of the iron-binding motif Glu-X-X-His, in the carboxy-terminal hydrophilic domain of the alternative oxidase that suggest the presence of a hydroxo-bridged binuclear iron center, analogous to that found in the enzyme methane monooxygenase. Using the known three-dimensional structures of other binuclear iron proteins, we have developed a structural model for the proposed catalytic site of the alternative oxidase based on these amino acid sequence similarities.

【 授权许可】

Unknown