Role of the hinge protein in the electron transfer between cardiac cytochrome c1 and c. Equilibrium constants and kinetic probes.
A role of the hinge protein is studied in the electron transfer reaction between cytochromes c1 and c, using highly purified "one-band" cytochrome c1 and "two-band" cytochrome c1. The results show that the hinge protein (Hp), which is essential for a stable ionic strength-sensitive c1-Hp-c complex, seems to play a certain role in electron transfer between cytochromes c1 and c; Keq for electron transfer reaction between cytochromes c1 and c in the presence of the hinge protein is found to be about 40% higher than that in the absence of the hinge protein at low ionic strength, but no difference exists at high ionic strength. We propose a hypothesis that the hinge protein may function as regulator for the electron transfer reaction between cytochromes c1 and c, and this may be at least one of the roles of the hinge protein in mitochondria.
D003574:Cytochrome c Group / Q000031:analogs & derivatives* / Q000378:metabolism*; D003575:Cytochromes c1 / Q000378:metabolism*; D004579:Electron Transport; D014450:Electron Transport Complex III; D007700:Kinetics; D009994:Osmolar Concentration; D011506:Proteins / Q000378:metabolism*
D003574:Cytochrome c Group; D011506:Proteins; C039762:UQCRH protein, human; D003575:Cytochromes c1; D014450:Electron Transport Complex III