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Reverse Electron Transfer by Respiratory Complex I Catalyzed in a Modular Proteoliposome System.
Wright, John J; Biner, Olivier; Chung, Injae; Burger, Nils; Bridges, Hannah R; Hirst, Judy.
Afiliação
  • Wright JJ; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
  • Biner O; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
  • Chung I; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
  • Burger N; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
  • Bridges HR; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
  • Hirst J; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, U.K.
J Am Chem Soc ; 144(15): 6791-6801, 2022 04 20.
Article em En | MEDLINE | ID: mdl-35380814
Respiratory complex I is an essential metabolic enzyme that uses the energy from NADH oxidation and ubiquinone reduction to translocate protons across an energy transducing membrane and generate the proton motive force for ATP synthesis. Under specific conditions, complex I can also catalyze the reverse reaction, Δp-linked oxidation of ubiquinol to reduce NAD+ (or O2), known as reverse electron transfer (RET). Oxidative damage by reactive oxygen species generated during RET underpins ischemia reperfusion injury, but as RET relies on several converging metabolic pathways, little is known about its mechanism or regulation. Here, we demonstrate Δp-linked RET through complex I in a synthetic proteoliposome system for the first time, enabling complete kinetic characterization of RET catalysis. We further establish the capability of our system by showing how RET in the mammalian enzyme is regulated by the active-deactive transition and by evaluating RET by complex I from several species in which direct assessment has not been otherwise possible. We thus provide new insights into the reversibility of complex I catalysis, an important but little understood mechanistic and physiological feature.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexo I de Transporte de Elétrons / Elétrons Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexo I de Transporte de Elétrons / Elétrons Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article