Binuclear centre structure of terminal protonmotive oxidases.
The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319, T326) into the vicinity of the binuclear centre, suggestive of a proton-transferring function. In addition, we also consider those residues which may participate in electron transport between CuA and haem a. We suggest several potential lines of investigation.
Brown
S
S
Glynn Research Institute, Bodmin, Cornwall, UK.
Moody
A J
AJ
Mitchell
R
R
Rich
P R
PR
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D055592:Biophysical Phenomena; D001703:Biophysics; D002384:Catalysis; D002417:Cattle; D003573:Cytochrome b Group / Q000737:chemistry; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry; D006418:Heme / Q000737:chemistry; D007473:Ion Channels; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011522:Protons; D016415:Sequence Alignment
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005656:Fungal Proteins; D007473:Ion Channels; D011522:Protons; D006418:Heme; D003576:Electron Transport Complex IV