Abstract
New experimental evidence that a switch controls the reduction of the heme a3-CuB binuclear centre has been observed in the N2-dried thin film of purified cytochrome oxidase. When immersing the enzyme film into the acid phosphate buffer with extremely low concentration of dithionite, a spectrum was given to show a reduction of heme a with no electrons resting on CuA. By increasing dithionite, electrons could be accumulated gradually on CuA, but the binuclear centre still remains in the oxidized state. When the accumulation of electrons on CuA and/or heme a exceeded a threshold, a turnover of reduction of the binuclear centre and oxidation of heme a occurred abruptly. This switch-like action is pH-dependent.
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 call
