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A revised model of the active site of alternative oxidase
Author(s) -
Andersson Martin E,
Nordlund Pär
Publication year - 1999
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/s0014-5793(99)00376-2
Subject(s) - carboxylate , chemistry , active site , biochemistry , homology modeling , structural motif , protein structure , stereochemistry , oxidase test , homology (biology) , enzyme , amino acid
The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. A structure of this protein has previously been proposed based on an assumed structural homology to the di‐iron carboxylate family of proteins. However, these authors suggested the protein has a very different topology than the known structures of di‐iron carboxylate proteins. We have re‐examined this model and based on comparison of recent sequences and structural data on di‐iron carboxylate proteins we present a new model of the alternative oxidase which allows prediction of active site residues and a possible membrane binding motif.