Mechanistic insight from the crystal structure of mitochondrial complex I

Author:

Zickermann Volker12,Wirth Christophe3,Nasiri Hamid45,Siegmund Karin1,Schwalbe Harald25,Hunte Carola3,Brandt Ulrich26

Affiliation:

1. Structural Bioenergetics Group, Institute of Biochemistry II, Medical School, Goethe-University, 60438 Frankfurt am Main, Germany.

2. Cluster of Excellence Frankfurt “Macromolecular Complexes,” Goethe-University, 60438 Frankfurt am Main, Germany.

3. Institute for Biochemistry and Molecular Biology, ZBMZ, BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.

4. Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

5. Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, 60438 Frankfurt am Main, Germany.

6. Nijmegen Center for Mitochondrial Disorders, Radboud University Medical Center, 6525 GA Nijmegen, Netherlands.

Abstract

Energy conversion in complex 1 ATP, the energy source of the cell, is synthesized by a protein residing in the mitochondrial inner membrane. The synthesis is driven by a proton gradient generated by redox reactions that transfer electrons between a series of enzymes in the membrane. The largest complex in this electron transfer chain is the 1-MD complex 1. It couples electron transfer from NADH to ubiquinone to the translocation of four protons. Zickermann et al. report the crystal structure of a complex comprising the 14 central subunits and the largest accessory subunit of mitochondrial complex 1 from a yeast-genetic model at 3.6 Å resolution. The structure identifies four potential proton translocation pathways and gives insight into how energy from the redox reactions is transmitted to drive proton pumping. Science , this issue p. 44

Funder

German Research Foundation

Excellence Initiative of the German Federal and State Governments

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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