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Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc1 function in vivo.

ABSTRACT: Electronic connection between Qo and Qi quinone catalytic sites of dimeric cytochrome bc1 is a central feature of the energy-conserving Q cycle. While both the intra- and inter-monomer electron transfers were shown to connect the sites in the enzyme, mechanistic and physiological significance of the latter remains unclear. Here, using a series of mutated hybrid cytochrome bc1-like complexes, we show that inter-monomer electron transfer robustly sustains the function of the enzyme in vivo, even when the two subunits in a dimer come from different species. This indicates that minimal requirement for bioenergetic efficiency is to provide a chain of cofactors for uncompromised electron flux between the catalytic sites, while the details of protein scaffold are secondary.

SUBMITTER: Ekiert R

PROVIDER: S-EPMC4152375 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc1 function in vivo.

Ekiert Robert R Czapla Monika M Sarewicz Marcin M Osyczka Artur A

Biochemical and biophysical research communications 20140801 2

Electronic connection between Qo and Qi quinone catalytic sites of dimeric cytochrome bc1 is a central feature of the energy-conserving Q cycle. While both the intra- and inter-monomer electron transfers were shown to connect the sites in the enzyme, mechanistic and physiological significance of the latter remains unclear. Here, using a series of mutated hybrid cytochrome bc1-like complexes, we show that inter-monomer electron transfer robustly sustains the function of the enzyme in vivo, even w ...[more]

PMID: 25089001

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