Citation

BibTex format

@article{Rutherford:2012:10.1016/j.febslet.2011.12.039,
author = {Rutherford, AW and Osyczka, A and Rappaport, F},
doi = {10.1016/j.febslet.2011.12.039},
journal = {FEBS Lett},
pages = {603--616},
title = {Back-reactions, short-circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O(2).},
url = {http://dx.doi.org/10.1016/j.febslet.2011.12.039},
volume = {586},
year = {2012}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The energy-converting redox enzymes perform productive reactions efficiently despite the involvement of high energy intermediates in their catalytic cycles. This is achieved by kinetic control: with forward reactions being faster than competing, energy-wasteful reactions. This requires appropriate cofactor spacing, driving forces and reorganizational energies. These features evolved in ancestral enzymes in a low O(2) environment. When O(2) appeared, energy-converting enzymes had to deal with its troublesome chemistry. Various protective mechanisms duly evolved that are not directly related to the enzymes' principal redox roles. These protective mechanisms involve fine-tuning of reduction potentials, switching of pathways and the use of short circuits, back-reactions and side-paths, all of which compromise efficiency. This energetic loss is worth it since it minimises damage from reactive derivatives of O(2) and thus gives the organism a better chance of survival. We examine photosynthetic reaction centres, bc(1) and b(6)f complexes from this view point. In particular, the evolution of the heterodimeric PSI from its homodimeric ancestors is explained as providing a protective back-reaction pathway. This "sacrifice-of-efficiency-for-protection" concept should be generally applicable to bioenergetic enzymes in aerobic environments.
AU - Rutherford,AW
AU - Osyczka,A
AU - Rappaport,F
DO - 10.1016/j.febslet.2011.12.039
EP - 616
PY - 2012///
SP - 603
TI - Back-reactions, short-circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O(2).
T2 - FEBS Lett
UR - http://dx.doi.org/10.1016/j.febslet.2011.12.039
VL - 586
ER -