Further insights into the structure of the alternative oxidase: from plants to parasites.
The AOX (alternative oxidase) is a non-protonmotive ubiquinol-oxygen oxidoreductase that couples the oxidation of ubiquinol with the complete reduction of water. Although it has long been recognized that it is ubiquitous among the plant kingdom, it has only recently become apparent that it is also widely found in other organisms including some human parasites. In this paper, we review experimental studies that have contributed to our current understanding of its structure, with particular reference to the catalytic site. Furthermore, we propose a model for the ubiquinol-binding site which identifies a hydrophobic pocket, between helices II and III, leading from a proposed membrane-binding domain to the catalytic domain.
Moore
Anthony L
AL
Biochemistry and Biomedical Sciences, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK. a.l.moore@sussex.ac.uk
Albury
Mary S
MS
D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation; D011809:Quinones / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D000099188:Alternative Oxidase
D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D010940:Plant Proteins; D011809:Quinones; D000099188:Alternative Oxidase