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Structure of Complex III with Bound Cytochrome c in Reduced State and Definition of a Minimal Core Interface for Electron Transfer

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Solmaz,  Sozanne R.N.
Department of Molecular Membrane 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;
Cluster of Excellence Macromolecular Complexes, Max Planck Institute of Biophysics, 60539 Frankfurt am Main, Germany;

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Citation

Solmaz, S. R., & Hunte, C. (2008). Structure of Complex III with Bound Cytochrome c in Reduced State and Definition of a Minimal Core Interface for Electron Transfer. Journal of Biological Chemistry, 283(25), 17542-17549. doi:10.1074/jbc.M710126200.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D83D-A
Abstract
In cellular respiration, cytochrome c transfers electrons from cytochrome bc1 complex (complex III) to cytochrome c oxidase by transiently binding to the membrane proteins. Here, we report the structure of isoform-1 cytochrome c bound to cytochrome bc1 complex at 1.9Å resolution in reduced state. The dimer structure is asymmetric. Monovalent cytochrome c binding is correlated with conformational changes of the Rieske head domain and subunit QCR6p and with a higher number of interfacial water molecules bound to cytochrome c1. Pronounced hydration and a “mobility mismatch” at the interface with disordered charged residues on the cytochrome c side are favorable for transient binding. Within the hydrophobic interface, a minimal core was identified by comparison with the novel structure of the complex with bound isoform-2 cytochrome c. Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex.