Characterization of mutations in crucial residues around the Q(o) binding site of the cytochrome bc complex from Paracoccus denitrificans

The FEBS Journal
Thomas KleinschrothPetra Hellwig

Abstract

The protonation state of residues around the Q(o) binding site of the cytochrome bc(1) 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 b(L) 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 signals from the oxidized quinone and of the protein backbone. By monitoring the interaction with the inhibitor stigmatellin for the wild-type enzyme at various redox states, interactions of the bound stigmatellin with amino acid side chains such as protonated acidic residues and the backbone were observed, as well as difference signals arising fro...Continue Reading

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Citations

Jul 16, 2014·Biochimica Et Biophysica Acta·Petra Hellwig
Mar 10, 2009·Biochimica Et Biophysica Acta·Oliver-Matthias H Richter, Bernd Ludwig
Aug 22, 2020·Chemical Reviews·Frederic Melin, Petra Hellwig
May 1, 2021·Frontiers in Chemistry·Filipa Calisto, Manuela M Pereira

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