Abstract
If cytochrome c oxidase is subjected to pressure during the aerobic steady state, large spectral changes are apparent. These seem to be associated with the inhibition of electron transport within the oxidase. The volume change for the transition is about 80 mL/mol. When the oxidase in the aerobic steady state, with porphyrin cytochrome c (the iron-free derivative of cytochrome c) bound to it, is subjected to pressure, the porphyrin derivative is released. This results from a change in the dissociation constant of the complex. Whereas the dissociation constant during turnover is about 1.25 X 10(-8) M, during pressure-induced inhibition the dissociation constant appears to be about an order of magnitude greater. It appears as though the binding site of the inhibited, partially reduced enzyme more closely resembles that of the fully reduced enzyme than that of the enzyme during the aerobic steady state.
Sign-in/Register to access full text options 
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.
