The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center
Open Access
- 27 March 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 362 (1) , 10-14
- https://doi.org/10.1016/0014-5793(95)00196-g
Abstract
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.Keywords
This publication has 26 references indexed in Scilit:
- The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductaseFEBS Letters, 1992
- Proteins containing oxo-bridged dinuclear iron centers: a bioinorganic perspectiveChemical Reviews, 1990
- Essential role of ferrous iron in cyanide‐resistant respiration in Hansenula anomalaFEBS Letters, 1990
- Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase componentJournal of the American Chemical Society, 1990
- Component of the alternative oxidase localized to the matrix surface of the inner membrane of plant mitochondriaFEBS Letters, 1990
- Electronic and Raman spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compoundsJournal of the American Chemical Society, 1989
- Structure of myohemerythrin in the azidomet state at resolutionJournal of Molecular Biology, 1987
- The alternative oxidase: A cyanide‐resistant respiratory pathway in higher plantsPhysiologia Plantarum, 1986
- Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphicsJournal of Molecular Biology, 1981
- Isolation of a cyanide‐resistant duroquinol oxidase from arum maculatum mitochondriaFEBS Letters, 1978