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Title: Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc{sub 1} function in vivo

Abstract

Highlights: • We used hybrid fusion bc{sub 1} complex to test inter-monomer electron transfer in vivo. • Cross-inactivated complexes were able to sustain photoheterotrophic growth. • Inter-monomer electron transfer supports catalytic cycle in vivo. • bc{sub 1} dimer is functional even when cytochrome b subunits come from different species. - Abstract: Electronic connection between Q{sub o} and Q{sub i} quinone catalytic sites of dimeric cytochrome bc{sub 1} 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 bc{sub 1}-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.

Authors:
; ; ;
Publication Date:
OSTI Identifier:
22416719
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 451; Journal Issue: 2; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; BENZOQUINONES; COMPLEXES; DIMERS; ELECTRON TRANSFER; ELECTRONS; ENERGY CONVERSION; ENZYMES; HYBRIDIZATION; IN VIVO; MITOCHONDRIA; MONOMERS

Citation Formats

Ekiert, Robert, Czapla, Monika, Sarewicz, Marcin, and Osyczka, Artur, E-mail: artur.osyczka@uj.edu.pl. Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc{sub 1} function in vivo. United States: N. p., 2014. Web. doi:10.1016/J.BBRC.2014.07.117.
Ekiert, Robert, Czapla, Monika, Sarewicz, Marcin, & Osyczka, Artur, E-mail: artur.osyczka@uj.edu.pl. Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc{sub 1} function in vivo. United States. doi:10.1016/J.BBRC.2014.07.117.
Ekiert, Robert, Czapla, Monika, Sarewicz, Marcin, and Osyczka, Artur, E-mail: artur.osyczka@uj.edu.pl. Fri . "Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc{sub 1} function in vivo". United States. doi:10.1016/J.BBRC.2014.07.117.
@article{osti_22416719,
title = {Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc{sub 1} function in vivo},
author = {Ekiert, Robert and Czapla, Monika and Sarewicz, Marcin and Osyczka, Artur, E-mail: artur.osyczka@uj.edu.pl},
abstractNote = {Highlights: • We used hybrid fusion bc{sub 1} complex to test inter-monomer electron transfer in vivo. • Cross-inactivated complexes were able to sustain photoheterotrophic growth. • Inter-monomer electron transfer supports catalytic cycle in vivo. • bc{sub 1} dimer is functional even when cytochrome b subunits come from different species. - Abstract: Electronic connection between Q{sub o} and Q{sub i} quinone catalytic sites of dimeric cytochrome bc{sub 1} 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 bc{sub 1}-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.},
doi = {10.1016/J.BBRC.2014.07.117},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 451,
place = {United States},
year = {Fri Aug 22 00:00:00 EDT 2014},
month = {Fri Aug 22 00:00:00 EDT 2014}
}