Abstract
Heme-copper respiratory oxidases are highly efficient molecular machines. These membrane enzymes catalyze the final stage of cellular respiration of eukaryotes and many prokaryotes: the transfer of electrons from cytochromes or quinols to molecular oxygen and the reduction of O2 to water. The free energy released in this redox reaction is converted by heme-copper respiratory oxidases into a transmembrane gradient of the electrochemical potential of hydrogen ions (ΔµH+). Heme-copper respiratory oxidases have a unique mechanism for generation ΔµH+ - a redox-coupled proton pump. The use of a combination of a direct electrometric method for measuring the kinetics of membrane potential generation with approaches and methods of prestationary kinetics and directed mutagenesis in the study of heme-copper oxidases makes it possible to obtain unique information about the movement of protons inside the protein in real time. The review summarizes the results of the use of the permitted time.
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