Abstract
A new purification method for cytochrome c oxidase, involving hydrophobic interaction chromatography, has been developed. Replacing the detergent in solubilized oxidase by phospholipid vesicles increases the catalytic activity concomitant with changes in spectroscopic and redox properties. Formate causes an increase in the magnetic susceptibility difference between oxidized and reduced oxidase, probably by disturbing the magnetic coupling between cytochrome α3 and Cuu. Ferricyanide affects the redox properties of the enzyme but a high-potential heme is found also in its absence. The rate of intramolecular electron transfer is increased in enzyme molecules that have undergone one catalytic cycle. Attempts to find an oxygen radical intermediate in the catalytic reaction with the aid of 170 have been unsuccessful.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
