tailieunhanh - Báo cáo khoa học: Characterization of mutations in crucial residues around the Qo binding site of the cytochrome bc1 complex from Paracoccus denitrificans

The protonation state of residues around the Qo binding site of the cyto-chrome bc1 complex from Paracoccus denitrificansand their interaction with bound quinone(s) was studied by a combined electrochemical and FTIR difference spectroscopic approach. Site-directed mutations of two groups of conserved residues were investigated: (a) acidic side chains located close to the surface and thought to participate in a water chain leading up to the heme bLedge, and (b) residues located in the vicinity of this site. . | ỊFEBS Journal Characterization of mutations in crucial residues around the Qo binding site of the cytochrome bc1 complex from Paracoccus denitrificans Thomas Kleinschroth1 Oliver Anderka1 Michaela Ritter2 Andreas Stocker1 2 Thomas A. Link2 Bernd Ludwig1 and Petra Hellwig3 1 Institut fur Biochemie der Johann Wolfgang Goethe Universitat Molekulare Genetik Biozentrum Frankfurt am Main Germany 2 Institut fur Biophysik der Johann Wolfgang Goethe Universitat Frankfurt am Main Germany 3 Institut de Chimie UMR 7177 CNRS Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolecules Universite Louis Pasteur Strasbourg France Keywords bc1 complex FTIR spectroscopy Paracoccus denitrificans proton and electron transfer quinones Correspondence P. Hellwig Institut de Chimie UMR 7177 CNRS Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolecules Universite Louis Pasteur 4 rue Blaise Pascal 67000 Strasbourg France Fax 33 390 241431 Tel 33 390 241273 E-mail hellwig@ Received 31 March 2008 revised 14 June 2008 accepted 28 July 2008 doi The protonation state of residues around the Qo binding site of the cytochrome bc1 complex from Paracoccus denitrificans and their interaction with bound quinone s was studied by a combined electrochemical and FTIR difference spectroscopic approach. Site-directed mutations of two groups of conserved residues were investigated a acidic side chains located close to the surface and thought to participate in a water chain leading up to the heme bL edge and b residues located in the vicinity of this site. Interestingly most of the mutants retain a high degree of catalytic activity. E295Q E81Q and Y297F showed reduced stigmatellin affinity. On the basis of electrochemically induced FTIR difference spectra we suggest that E295 and D278 are protonated in the oxidized form or that their mutation perturbs protonated residues. Mutations Y302 Y297 E81 and E295 directly perturb

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