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The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center
Author(s) -
Siedow James N.,
Umbach Ann L.,
Moore Anthony L.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00196-g
Subject(s) - cyanide , oxidase test , chemistry , active center , alternative oxidase , stereochemistry , amino acid , biochemistry , active site , enzyme , methane monooxygenase , oxidoreductase , catalysis , cytochrome c oxidase , mitochondrion , organic chemistry
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.