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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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Published in: | Biochemistry (Moscow) 2023-10, Vol.88 (10), p.1513-1527 |
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description | 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. |
doi_str_mv | 10.1134/S0006297923100085 |
format | article |
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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.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297923100085</identifier><identifier>PMID: 38105021</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Amino acids ; Analysis ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Copper ; Copper converters ; Cytochrome ; Electrochemical potential ; Electrochemistry ; Enzymes ; Eukaryotes ; Free energy ; Heme ; Hydrogen bonds ; Hydrogen ions ; Kinetics ; Life Sciences ; Measurement methods ; Membrane potential ; Membrane potentials ; Membranes ; Microbiology ; Mitochondria ; Molecular machines ; Oxidases ; Oxygen ; Prokaryotes ; Proteins ; Protons ; Real time ; Redox reactions ; Review ; Site-directed mutagenesis ; Translocation</subject><ispartof>Biochemistry (Moscow), 2023-10, Vol.88 (10), p.1513-1527</ispartof><rights>Pleiades Publishing, Ltd. 2023</rights><rights>COPYRIGHT 2023 Springer</rights><rights>Pleiades Publishing, Ltd. 2023.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c391t-81f3720ad8f200435585e7579297e438009f5beee8de7f25c2a9aab04d2350883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38105021$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siletsky, Sergei A.</creatorcontrib><title>Investigation of the Mechanism of Membrane Potential Generation by Heme-Copper Respiratory Oxidases in a Real Time Mode</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>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.</description><subject>Amino acids</subject><subject>Analysis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Copper</subject><subject>Copper converters</subject><subject>Cytochrome</subject><subject>Electrochemical potential</subject><subject>Electrochemistry</subject><subject>Enzymes</subject><subject>Eukaryotes</subject><subject>Free energy</subject><subject>Heme</subject><subject>Hydrogen bonds</subject><subject>Hydrogen ions</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Measurement methods</subject><subject>Membrane potential</subject><subject>Membrane potentials</subject><subject>Membranes</subject><subject>Microbiology</subject><subject>Mitochondria</subject><subject>Molecular machines</subject><subject>Oxidases</subject><subject>Oxygen</subject><subject>Prokaryotes</subject><subject>Proteins</subject><subject>Protons</subject><subject>Real time</subject><subject>Redox reactions</subject><subject>Review</subject><subject>Site-directed 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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.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><pmid>38105021</pmid><doi>10.1134/S0006297923100085</doi><tpages>15</tpages></addata></record> |
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subjects | Amino acids Analysis Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Copper Copper converters Cytochrome Electrochemical potential Electrochemistry Enzymes Eukaryotes Free energy Heme Hydrogen bonds Hydrogen ions Kinetics Life Sciences Measurement methods Membrane potential Membrane potentials Membranes Microbiology Mitochondria Molecular machines Oxidases Oxygen Prokaryotes Proteins Protons Real time Redox reactions Review Site-directed mutagenesis Translocation |
title | Investigation of the Mechanism of Membrane Potential Generation by Heme-Copper Respiratory Oxidases in a Real Time Mode |
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