STRUCTURE-FUNCTION-RELATIONSHIPS OF THE ALTERNATIVE OXIDASE OF PLANT-MITOCHONDRIA - A MODEL OF THE ACTIVE-SITE

被引：83

作者：

MOORE, AL ^{[1
]}

UMBACH, AL ^{[1
]}

SIEDOW, JN ^{[1
]}

机构：

[1] DUKE UNIV,DCMB BOT,DURHAM,NC 27708

来源：

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 1995年 / 27卷 / 04期

关键词：

ALTERNATIVE OXIDASE; SEQUENCE HOMOLOGY; HYDROXO-BRIDGED DIIRON CENTER PROTEINS; MITOCHONDRIA;

D O I：

10.1007/BF02109999

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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.

引用

页码：367 / 377

页数：11

共 68 条

[1] STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER-SPHAEROIDES R-26 - PROTEIN COFACTOR (QUINONES AND FE-2+) INTERACTIONS .5. [J].