THERMODYNAMIC STUDIES OF ELECTRON AND PROTON AFFINITIES OF CYTOCHROMES
Project Number1Z01HL000401-20
Contact PI/Project LeaderHENDLER, R W
Awardee OrganizationNATIONAL HEART, LUNG, AND BLOOD INSTITUTE
Description
Abstract Text
Many theoretical issues were raised by our newer findings on the spectral
and thermodynamic characterization of cytochrome aa3. Our finding that CO
did not raise the Em of cytochrome a3 is contrary to theory for a case
where a ligand binds more strongly to the reduced member of a redox
couple. We proposed that protons are second ligands that bind more
strongly to the oxidized member of the CO-liganded couple. A theoretical
paper published early this year using other considerations reached the
opposite conclusion. In an intensive theoretical examination of
cooperativity for a system involving three ligands (electron, proton, and
CO), we were able to explain how the later results do not rule out
cooperative interactions involving protons and how multi-ligand
interactions could be effectively utilized for a redox-drive Bohr-type
proton pump. Other of our newer findings posed additional theoretical
questions. We concluded that the redox potential of cytochrome a3 was
under the control of the redox state of other centers in the molecule. We
found that lowering the voltage first oxidized cytochrome a3 and then
reduced it. Existing theory does not account for these phenomena.
Cytochrome oxidase can theoretically possess from 4 to 13 redox centers.
The Em of any center may be cooperatively affected by any combination of
electrons in the other centers. We have started a quantitative theoretical
consideration of the expected effects of redox interactions in a variety of
possible models based on cytochrome oxidase. Preliminary results indicate
that redox cooperativity can account for our newer results. A research
collaboration was initiated with the laboratory of Britton Chance. Our
newer intensive analytical techniques, in equilibrium studies, revealed
specific spectral components and interactions. We hope to use the same
analytical technique in kinetic studies coupled with our newer
characterizations of the components to study the mechanism of cytochrome
oxidase activity. Preliminary results do show the same kinds of spectra we
had encountered in our work.
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