Models for structure and function in quinone-binding sites: the Escherichia coli quinol oxidase, cytochrome bo3.
School of Biological and Medical Sciences, University of St. Andrews, Scotland, UK.
L
L
Murray
R H
RH
Pires
S F
SF
Hastings
W J
WJ
Ingledew
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry* / Q000502:physiology*; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry* / Q000502:physiology; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; C083850:cytochrome bo3, E coli; D010088:Oxidoreductases; C020094:duroquinol oxidase