Abstract
Bovine serum albumin (BSA) at micromolar concentrations causes a red shift of the Sorer band of bovine cytochrome c oxidase with a slow biphasic time course. It also inhibits the turnover of detergent-isolated enzyme in a similarly slow manner; the progress of this inhibition is halted by palmitate and other fatty acids. The inhibitory bovine serum albumin effect may involve fatty acid depletion from the enzyme. Respiration by cytochrome c oxidase vesicles (proteoliposomes) in the presence of ionophores (uncontrolled) shows only a small inhibition by BSA but preincubation of such vesicles with BSA induces a loss of proton pumping activity. After incubation of BSA-depleted proteoliposomes in the presence of reductant with combinations of fatty acids, pumping activity can be fully restored, suggesting a supportive or even essential role of endogenous fatty acids in H+ translocation by this membranous enzyme.
Original language | English (US) |
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Pages (from-to) | 134-138 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 391 |
Issue number | 1-2 |
DOIs | |
State | Published - Aug 5 1996 |
Keywords
- Bovine serum albumin
- Cytochrome c oxidase
- Fatty acids
- Oleate
- Palmitate
- Proteoliposomes
- Proton pumping
- Respiratory control
- Spectral change
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology