Investigation of the Mechanism of Membrane Potential Generation by Heme-Copper Respiratory Oxidases in a Real Time Mode

Heme-copper respiratory oxidases are highly efficient molecular machines. These membrane enzymes catalyze the final step of cellular respiration in eukaryotes and many prokaryotes: the transfer of electrons from cytochromes or quinols to molecular oxygen and oxygen reduction to water. The free energ...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2023-10, Vol.88 (10), p.1513-1527
Main Author: Siletsky, Sergei A.
Format: Article
Language:English
Subjects:
Amino acids
Analysis
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Ceruloplasmin - metabolism
Copper
Copper converters
Cytochrome
Electrochemical potential
Electrochemistry
Electron Transport Complex IV - metabolism
Enzymes
Eukaryotes
Free energy
Heme
Heme - chemistry
Hydrogen bonds
Hydrogen ions
Kinetics
Life Sciences
Measurement methods
Membrane potential
Membrane Potentials
Membranes
Microbiology
Mitochondria
Molecular machines
Oxidases
Oxidation-Reduction
Oxidoreductases - metabolism
Oxygen
Oxygen - metabolism
Prokaryotes
Proteins
Protons
Real time
Redox reactions
Review
Site-directed mutagenesis
Translocation
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Summary:Heme-copper respiratory oxidases are highly efficient molecular machines. These membrane enzymes catalyze the final step of cellular respiration in eukaryotes and many prokaryotes: the transfer of electrons from cytochromes or quinols to molecular oxygen and oxygen reduction to water. The free energy released in this redox reaction is converted by heme-copper respiratory oxidases into the transmembrane gradient of the electrochemical potential of hydrogen ions Δ μ H+ ). Heme-copper respiratory oxidases have a unique mechanism for generating Δ μ H + , namely, a redox-coupled proton pump. A combination of direct electrometric method for measuring the kinetics of membrane potential generation with the methods of prestationary kinetics and site-directed mutagenesis in the studies of heme-copper oxidases allows to obtain a unique information on the translocation of protons inside the proteins in real time. The review summarizes the data of studies employing time-resolved electrometry to decipher the mechanisms of functioning of these important bioenergetic enzymes.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297923100085