Autor: |
Grba DN, Wright JJ, Yin Z, Fisher W, Hirst J; Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK. |
Jazyk: |
angličtina |
Zdroj: |
Science (New York, N.Y.) [Science] 2024 Jun 14; Vol. 384 (6701), pp. 1247-1253. Date of Electronic Publication: 2024 Jun 13. |
DOI: |
10.1126/science.ado2075 |
Abstrakt: |
Respiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and cellular damage. Ischemic conditions switch complex I from rapid, reversible catalysis into a dormant state that protects upon reoxygenation, but the molecular basis for the switch is unknown. We combined precise biochemical definition of complex I catalysis with high-resolution cryo-electron microscopy structures in the phospholipid bilayer of coupled vesicles to reveal the mechanism of the transition into the dormant state, modulated by membrane interactions. By implementing a versatile membrane system to unite structure and function, attributing catalytic and regulatory properties to specific structural states, we define how a conformational switch in complex I controls its physiological roles. |
Databáze: |
MEDLINE |
Externí odkaz: |
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