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J. Biol. Chem., Vol. 266, Issue 4, 2219-2226, Feb, 1991
BC Hill
The reaction of the electrostatic cytochrome c-cytochrome oxidase complex
with oxygen is measured by transient absorption spectroscopy. The oxygen
reaction is initiated by photolytic removal of CO from cytochrome oxidase,
using a flash-pumped dye laser. The subsequent reaction of the cytochrome
c-cytochrome oxidase complex with oxygen is reported at 550, 605, 744, and
830 nm at different cytochrome c:cytochrome oxidase ratios and different
oxygen concentrations. In the absence of cytochrome c the time course of
the reaction of the oxidase is well described by a triple exponential
process at any of the measured wavelengths. The three processes are well
resolved at high O2 levels (i.e. greater than 200 microM), where they reach
first-order rate limits of 2.4 x 10(4), 7.5 x 10(3), and 650 s-1. When
cytochrome c is added the oxidation of cytochrome a and one of the redox
active cooper centers (CuA) are interrupted. The maximal effect of
cytochrome c on the oxidation of the oxidase occurs at a c:aa3 ratio of 1.
Cytochrome c reacts in a biphasic process with rates of up to 7 x 10(3) and
550 s-1 at high oxygen. The fast phase takes up 60% of the process, and
this is independent of the cytochrome c:cytochrome oxidase ratio. The
results are discussed in the context of a model in which electron entry
into cytochrome oxidase from cytochrome c is via CuA, and cytochrome a
functions to mediate electron transfer from CuA to the oxygen binding site.
The role of CuA as initial electron acceptor in cytochrome c oxidase is
related to its physical proximity to cytochrome c is the cytochrome
c-cytochrome oxidase complex.
The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen
Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada.
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