The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center.
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.
Siedow
J N
JN
Duke University, Durham, NC 27708-1000, USA.
Umbach
A L
AL
Moore
A L
AL
D000595:Amino Acid Sequence; D001665:Binding Sites; D003486:Cyanides / Q000494:pharmacology; D007501:Iron / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D010940:Plant Proteins; D010944:Plants / Q000201:enzymology*; D017433:Protein Structure, Secondary; D014867:Water / Q000378:metabolism; D000099188:Alternative Oxidase
D003486:Cyanides; D007501:Iron; D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D010100:Oxygen; D010940:Plant Proteins; D014867:Water; D000099188:Alternative Oxidase