title: Structure of caa(3) cytochrome c oxidase--a nature-made enzyme-substrate complex.
abstract: Aerobic respiration, the energetically most favorable metabolic reaction, depends on the action of terminal oxidases that include cytochrome c oxidases. The latter forms a part of the heme-copper oxidase superfamily and consists of three different families (A, B, and C types). The crystal structures of all families have now been determined, allowing a detailed structural comparison from evolutionary and functional perspectives. The A2-type oxidase, exemplified by the Thermus thermophilus caa(3) oxidase, contains the substrate cytochrome c covalently bound to the enzyme complex. In this article, we highlight the various features of caa(3) enzyme and provide a discussion of their importance, including the variations in the proton and electron transfer pathways.
authors: Department of Chemical and Environmental Sciences and Materials and Surface Science Institute (MSSI), University of Limerick, Limerick, Ireland.
authors: Mohamed Radzi
authors: MR
authors: Noor
authors: Tewfik
authors: T
authors: Soulimane
mesh_terms: D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D045264:Cytochromes a / Q000737:chemistry* / Q000378:metabolism; D045266:Cytochromes a3 / Q000737:chemistry* / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013379:Substrate Specificity; D016963:Thermus thermophilus / Q000201:enzymology
chemical_list: D003574:Cytochrome c Group; D045266:Cytochromes a3; C435384:cytochrome caa(3); D045264:Cytochromes a; D003576:Electron Transport Complex IV