Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site.
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.
Moore
A L
AL
Department of Biochemistry, University of Sussex, Falmer, Brighton, U.K.
Umbach
A L
AL
Siedow
J N
JN
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D008928:Mitochondria / Q000201:enzymology*; D024101:Mitochondrial Proteins; D008961:Models, Structural; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D000099188:Alternative Oxidase
D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D010940:Plant Proteins; D000099188:Alternative Oxidase