Rieske/Cytochrome b Complexes: The Turbo Chargers of Chemiosmosis
Abstract
Rieske/cytochrome b complexes are transmembrane enzymes of many bioenergetic reaction chains. They operate according to a Q-cycle mechanism that allows the transfer of an extra proton over the membrane per electron transferred along the chain. Thus they optimize the ATP yield from the terminal electron donor/acceptor couples of the respective reaction chains. Two members of this family of enzymes, cytochrome bc 1 complex from proteobacteria and mitochondria and cytochrome b 6 f complex from cyanobacteria and chloroplast are well studied and crystal structures are available. While revealing unexpected features of the complexes, as the domain movement of the Rieske iron/sulfur protein and the presence of an unusual heme cofactor in a quinone binding pocket, they opened up new questions concerning the function of the enzyme. Few structural and functional studies are available for Rieske/cytb complexes from further species, which is the vast majority of bacterial and archeael phyla, and most information comes from genome analysis. Here we discuss structure and function of the complex from an evolutionary perspective.
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BibTeX
@article{brink2026rieskecytochrome,
title = {{Rieske/Cytochrome b Complexes: The Turbo Chargers of Chemiosmosis}},
author = {Felix Ten Brink and Frauke Baymann},
journal = {Advances in Photosynthesis and Respiration},
year = {2026},
month = sep,
doi = {10.1007/978-94-017-8742-0_8},
url = {https://hal.science/hal-05741382v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Rieske/Cytochrome b Complexes: The Turbo Chargers of Chemiosmosis
AU - Felix Ten Brink
AU - Frauke Baymann
PY - 2026
DA - 2026/09/07
JO - Advances in Photosynthesis and Respiration
DO - 10.1007/978-94-017-8742-0_8
UR - https://hal.science/hal-05741382v1
AB - Rieske/cytochrome b complexes are transmembrane enzymes of many bioenergetic reaction chains. They operate according to a Q-cycle mechanism that allows the transfer of an extra proton over the membrane per electron transferred along the chain. Thus they optimize the ATP yield from the terminal electron donor/acceptor couples of the respective reaction chains. Two members of this family of enzymes, cytochrome bc 1 complex from proteobacteria and mitochondria and cytochrome b 6 f complex from cyanobacteria and chloroplast are well studied and crystal structures are available. While revealing unexpected features of the complexes, as the domain movement of the Rieske iron/sulfur protein and the presence of an unusual heme cofactor in a quinone binding pocket, they opened up new questions concerning the function of the enzyme. Few structural and functional studies are available for Rieske/cytb complexes from further species, which is the vast majority of bacterial and archeael phyla, and most information comes from genome analysis. Here we discuss structure and function of the complex from an evolutionary perspective.
SN - 1572-0233
SN - 2215-0102
ER -