Functional Modules and Structural Basis of Conformational Coupling in Mitochondrial Complex I

Author:

Hunte Carola123,Zickermann Volker4,Brandt Ulrich4

Affiliation:

1. Institute for Biochemistry and Molecular Biology, Centre for Biological Signalling Studies (BIOSS), University of Freiburg, D-79104 Freiburg, Germany.

2. Institute of Membrane and Systems Biology, University of Leeds, Leeds LS2 9JT, UK.

3. Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt am Main, Germany.

4. Molecular Bioenergetics Group, Medical School, Cluster of Excellence Frankfurt “Macromolecular Complexes,” Center for Membrane Proteomics, Goethe-University, D-60596 Frankfurt am Main, Germany.

Abstract

Complex I Under Scrutiny Mitochondrial complex I is a large macromolecular membrane complex that couples electron transfer to proton pumping across the mitochondrial membrane and helps to drive adenosine 5′-triphosphate synthesis. Hunte et al. (p. 448 , published online 1 July) now describe the structure of complex 1 from the aerobic yeast, Yarrowia lipolytica . The sites involved in redox chemistry are distant from those that pump protons, and the structure suggests that a 60-angstrom-long helix is involved in transducing energy to the proton-pumping elements.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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