The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1

Author:

Francia Francesco,Malferrari Marco,Lanciano Pascal,Steimle Stefan,Daldal Fevzi,Venturoli Giovanni

Funder

NIH

MIUR

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference76 articles.

1. Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function;Xia;Biochim. Biophys. Acta Bioenerg.,2013

2. Possible molecular mechanism of the protonmotive function of cytochrome systems;Mitchell;J. Theor. Biol.,1976

3. The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex;Crofts;Biochim. Biophys. Acta Bioenerg.,2013

4. Reaction-center-driven cytochrome interactions in electron and proton translocation and energy coupling;Dutton,1978

5. Reaction center and UQH2:cyt c2 oxidoreductase act as independent enzymes in Rps. sphaeroides;Crofts;J. Bioenerg. Biomembr.,1986

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