TY  - JOUR
A1  - Zickermann, Volker
A1  - Bostina, Mihnea
A1  - Hunte, Carola
A1  - Ruiz, Teresa
A1  - Radermacher, Michael
A1  - Brandt, Ulrich
T1  - Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase
T2  - Journal of biological chemistry
N2  - Membrane-bound complex I (NADH:ubiquinone oxidoreductase) of the respiratory chain is considered the main site of mitochondrial radical formation and plays a major role in many mitochondrial pathologies. Structural information is scarce for complex I, and its molecular mechanism is not known. Recently, the 49-kDa subunit has been identified as part of the "catalytic core" conferring ubiquinone reduction by complex I. We found that the position of the 49-kDa subunit is clearly separated from the membrane part of complex I, suggesting an indirect mechanism of proton translocation. This contradicts all hypothetical mechanisms discussed in the field that link proton translocation directly to redox events and suggests an indirect mechanism of proton pumping by redox-driven conformational energy transfer.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76048
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-760486
SN  - 0021-9258
VL  - 278.2003
IS  - 31
SP  - 29072
EP  - 29078
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -