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

Hunte, Carola; Zickermann, Volker; Brandt, Ulrich

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

Hunte, C., Zickermann, V., & Brandt, U. (2010). Functional Modules and Structural Basis of Conformational Coupling in Mitochondrial Complex I. Science, 329, 448-451.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D690-9 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D692-5

Genre: Journal Article

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Creators:
Hunte, Carola¹, Author
Zickermann, Volker, Author
Brandt, Ulrich, Author

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1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290

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Abstract: Proton-pumping respiratory complex I is one of the largest and most complicated membrane protein complexes. Its function is critical for efficient energy supply in aerobic cells, and malfunctions are implicated in many neurodegenerative disorders. Here, we report an x-ray crystallographic analysis of mitochondrial complex I. The positions of all iron-sulfur clusters relative to the membrane arm were determined in the complete enzyme complex. The ubiquinone reduction site resides close to 30 angstroms above the membrane domain. The arrangement of functional modules suggests conformational coupling of redox chemistry with proton pumping and essentially excludes direct mechanisms. We suggest that a ~60-angstrom-long helical transmission element is critical for transducing conformational energy to proton-pumping elements in the distal module of the membrane arm.

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Language(s): eng - English

Dates: Date issued: 2010-07-23

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 530618

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Title: Science

Source Genre: Journal

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Pages: - Volume / Issue: 329 Sequence Number: - Start / End Page: 448 - 451 Identifier: -