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X-ray structure of the dimeric cytochrome bc1 complex from the soil bacterium Paracoccus denitrificans at 2.7-Å resolution

DOI: 10.1016/j.bbabio.2011.09.017 DOI Help
PMID: 21996020 PMID Help

Authors: Thomas Kleinschroth (University of Leeds) , Michela Castellani (Institute of Biochemistry, Molecular Genetics, Goethe University) , Chi Hung Trinh (Institute of Molecular and Cellular Biology, University of Leeds) , Nina Morgner (Goethe University) , Bernhard Brutschy (Goethe University) , Bernd Ludwig (Goethe University) , Carola Hunte (Institute for Biochemistry and Molecular Biology, ZMBZ, BIOSS Centre for Biological Signalling Studies)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochimica Et Biophysica Acta (bba) - Bioenergetics

State: Published (Approved)
Published: October 2011

Abstract: The respiratory cytochrome bc1 complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of proton motive force which fuels ATP synthesis. The complex from the ?-proteobacterium Paracoccus denitrificans, a model for the medically relevant mitochondrial complexes, lacked structural characterization. We show by LILBID mass spectrometry that truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer. The fully functional complex was crystallized and the X-ray structure determined at 2.7-Å resolution. It has high structural homology to mitochondrial complexes and to the Rhodobacter sphaeroides complex especially for subunits cytochrome b and ISP. Species-specific binding of the inhibitor stigmatellin is noteworthy. Interestingly, cytochrome c1 shows structural differences to the mitochondrial and even between the two Rhodobacteraceae complexes. The structural diversity in the cytochrome c1 surface facing the ISP domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. A similar position of the acidic N-terminal domains of cytochrome c1 and yeast subunit QCR6p is suggested in support of a similar function. A model of the electron transfer complex with membrane-anchored cytochrome c552, the natural substrate, shows that it can adopt the same orientation as the soluble substrate in the yeast complex. The full structural integrity of the P. denitrificans variant underpins previous mechanistic studies on intermonomer electron transfer and paves the way for using this model system to address open questions of structure/function relationships and inhibitor binding.

Journal Keywords: Anti-Bacterial; Crystallography; X-Ray; Dimerization; Electron; Electron; Models; Molecular; Molecular; Paracoccus; Polyenes; Protein; Soil Microbiology

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

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