Relationships between membrane-bound cytochrome o from Vitreoscilla and that of Escherichia coli.
The cytochrome o terminal oxidases from the bacteria Vitreoscilla and Escherichia coli are structurally and functionally related. They have similar optical spectra, both exhibit ubiquinol-1 oxidase activity and are inhibited similarly. Both enzymes contain four subunits by SDS-polyacrylamide gel electrophoresis analysis and contain protoheme IX and Cu2+ prosthetic groups. Antibodies raised against the oxidase purified from E. coli crossreact with the Vitreoscilla oxidase.
Georgiou
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CD
Department of Chemistry, University of Illinois, Urbana-Champaign 61801.
Cokic
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P
Carter
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Webster
D A
DA
Gennis
R B
RB
D000907:Antibodies, Bacterial / Q000276:immunology; D001419:Bacteria / Q000201:enzymology* / Q000276:immunology; D001426:Bacterial Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D003429:Cross Reactions; D003573:Cytochrome b Group; D003580:Cytochromes / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000276:immunology; D029968:Escherichia coli Proteins; D013045:Species Specificity; D014451:Ubiquinone / Q000031:analogs & derivatives / Q000378:metabolism
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D014451:Ubiquinone; C017168:cytochrome bo, E coli; C003741:ubiquinol