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Spectral evidence for the existence of a 2nd cytochrome o in whole cells of vitreoscilla

, : Spectral evidence for the existence of a 2nd cytochrome o in whole cells of vitreoscilla. Journal of Biological Chemistry 258(22): 13768-13771

Cytochrome o, a protoheme IX pigment, is proposed as the terminal oxidase of the filamentous bacterium, Vitroscilla. Aerobic and anaerobic photolysis of CO-liganded whole cells demonstrated the presence of a second CO-reactive pigment, cytochrome o' At temperatures lower than C, anaerobic photolysis dissociated only .apprx. 25% of the total CO-liganded components to reveal the unliganded cytochrome o'. At these temperatures, the photolysis of cytochrome o could not be demonstrated. At warmer temperatures, recombination of CO with the reduced cytochrome o' occurred with an apparent energy of activation of 5.8 kcol/mol. Aerobic photolysis of whole cells demonstrated 2 O-bound intermediates. At temperatures lower than C, a spectrally distinct compound with absorption maxima at 428, 534 and 564 nm appeared (form I'); the apparent second order rate constant (k+1) for the formation of this intermediate was 9.1 M-1 s-1, the reverse rate (k-1) was 9.9 .times. 10-5 s-1 and the equilibrium constant (Kd) was 1.1 .times. 10-5 M. This O intermediate of cytochrome o' is spectrally and kinetically similar to the O intermediate of cytochrome o seen in Escherichia coli. At temperatures warmer than C, photolysis of aerobic samples resulted in the immediate formation of a second O-bound intermediate (form I) with absorption maxima at 422, 534 and 564 nm. This second intermediate results from the binding of O to the cytochrome o (oxygenated cytochrome o). These data support the proposal that whole cells of Vitreoscilla contain 2 alternative pathways of electron transport, one terminating with cytochrome o and the other with cytochrome o'.

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