title: Proton translocation by bacteriorhodopsin and heme-copper oxidases.
abstract: Proton translocation is the means by which free energy is conserved from oxygen reduction by the respiratory heme-copper oxidases and from sunlight by bacteriorhodopsin. Three-dimensional structures at atomic resolution of both proteins have aided functional studies of the proton translocation mechanism. A comparison reveals common structural and functional features that may be unique to the primary proton pumps in biology.
authors.affiliation: Helsinki Bioenergetics Group, University of Helsinki, Finland. Marten.Wikstrom@Helsinki.Fi
authors.forename: M
authors.initials: M
authors.lastname: Wikström
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D015221:Potassium Channels / Q000378:metabolism; D017494:Proton Pumps / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D014867:Water / Q000378:metabolism
chemical_list: D015221:Potassium Channels; D017494:Proton Pumps; D011522:Protons; D014867:Water; D006418:Heme; D001436:Bacteriorhodopsins; D003300:Copper; D010088:Oxidoreductases