The three-spin intermediate at the O–O cleavage and proton-pumping junction in heme–Cu oxidases

Autor:	Ziqiao Ding, Antonio C. Roveda, Edward I. Solomon, Andrew W. Schaefer, Sylvia K. Choi, Wesley J. Transue, Anex Jose, Robert B. Gennis
Rok vydání:	2021
Předmět:	Hemeproteins Multidisciplinary Proton Cellular respiration Escherichia coli Proteins Proton Pumps Cytochrome b Group Photochemistry Cleavage (embryo) Article Electron Transport Complex IV Coupling (electronics) chemistry.chemical_compound chemistry Catalytic Domain Molecular oxygen Oxidoreductases Spin (physics) Adenosine triphosphate Heme Copper
Zdroj:	Science
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.abh3209
Popis:	Breaking down oxygen Molecular oxygen (O 2 ) is the terminal oxidant for respiration in mitochondria and many bacteria. Within membrane-bound heme–copper oxidases, a controlled, four-electron reduction of O 2 to water is coupled to pumping of protons across the membrane that can be used, among other outcomes, to generate adenosine triphosphate. Studying cytochrome bo 3 ubiquinol oxidase, Jose et al . investigated the key P M intermediate, which forms after O–O bond cleavage and precedes proton pumping, using magnetic circular dichroism spectroscopy. The authors observed features demonstrating that P M is a three-spin system, which is consistent with a consensus model including an iron(IV)-oxo species, copper(II) ion, and tyrosyl radical. These results provide an important validation of the O–O cleavage mechanism and open the door to understanding the proton pumping step. —MAF
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ea2183f0460c6aabac09e3f2550d4f https://doi.org/10.1126/science.abh3209 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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