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Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase

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Bostina,  Mihnea
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hunte,  Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ruiz,  Teresa
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Radermacher,  Michael
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Zickermann, V., Bostina, M., Hunte, C., Ruiz, T., Radermacher, M., & Brandt, U. (2003). Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase. The Journal of Biological Chemistry, 278(31), 29072-29078. doi:10.1074/jbc.M302713200.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB98-F
Abstract
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.