The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex.
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TLDR
The purpose of this review is to explain the protonmotive Q cycle, one of the most important mechanisms of cellular energy transduction, found in a phylogenetically diverse range of organisms.About:
This article is published in Journal of Biological Chemistry.The article was published on 1990-07-15 and is currently open access. It has received 579 citations till now. The article focuses on the topics: Q cycle & Coenzyme Q – cytochrome c reductase.read more
Citations
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Biochemistry and molecular cell biology of diabetic complications
TL;DR: This integrating paradigm provides a new conceptual framework for future research and drug discovery in diabetes-specific microvascular disease and seems to reflect a single hyperglycaemia-induced process of overproduction of superoxide by the mitochondrial electron-transport chain.
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The pathobiology of diabetic complications: a unifying mechanism.
TL;DR: What was learned about the pathobiology of diabetic complications starting with that 1966 Science paper and continuing through the end of the 1990s are described, including a unified mechanism that links together all of the seemingly unconnected pieces of the puzzle.
Journal ArticleDOI
Mitochondrial formation of reactive oxygen species.
TL;DR: This review describes the main mitochondrial sources of reactive species and the antioxidant defences that evolved to prevent oxidative damage in all the mitochondrial compartments and discusses various physiological and pathological scenarios resulting from an increased steady state concentration of mitochondrial oxidants.
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Oxidative stress and diabetic complications
TL;DR: Athrosclerosis and cardiomyopathy in type 2 diabetes are caused in part by pathway-selective insulin resistance, which increases mitochondrial ROS production from free fatty acids and by inactivation of antiatherosclerosis enzymes by ROS.
superoxide production blocks three pathways of hyperglycaemic damage
Takeshi Nishikawa,Diane Edelstein,Xue Liang Du,Sho-ichi Yamagishi,Takeshi Matsumura,Yasufumi Kaneda,Mark A. Yorek,David Beebek,Peter J. Oatesk,Hans-Peter Hammes,Ida Giardino,Michael Brownlee +11 more
TL;DR: This paper showed that hyperglycaemia increases the production of reactive oxygen species inside cultured bovine aortic endothelial cells and that this increase in reactive oxygen can be prevented by an inhibitor of electron transport chain complex II, an uncoupler of oxidative phosphorylation, by uncoupling protein-1 and by manganese superoxide dismutase.
References
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Possible molecular mechanisms of the protonmotive function of cytochrome systems.
TL;DR: The newly introduced concepts of the protonmotive ubiquinone cycle, or Q cycle, and of the cyclic loop 2–3 system, which represent developments of the redox loop concept, are shown to provide a promising basis for the evolution of a satisfactory theory.
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Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: protonmotive ubiquinone cycle.
TL;DR: The protonmotive Q* cycle is described, both for explaining the protontranslocating function of the cytochrome b-cl segment of the respiratory chain, and for rationalising much of the biochemical information about the behaviour and functions of the b cytochromes and ubiquinone, which previously appeared to be difficult to interpret simply.
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Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.
TL;DR: Calculation of the distribution of hydrophobic residues with a "hydropathy" function that is conserved in this family of proteins implies that the membrane-folding pattern of the 42-kilodalton (kDa) mitochondrial cytochromes involves 8-9 membrane-spanning domains.
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Cytochrome bc1 complexes of microorganisms.
TL;DR: The cytochrome bc1 complex is the most widely occurring electron transfer complex capable of energy transduction and the mechanism which links proton translocation to electron transfer through these proteins appears to be universal to all bc1 complexes.
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Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate . cytochrome c reductase complex.
T Ohnishi,B L Trumpower +1 more
TL;DR: It is proposed that a second site exists for binding of ubisemiquinone, which gives rise to a more slowly relaxing EPR signal which is abolished by antimycin, and that this site is identical with or closely related to the antimYcin binding site in the cytochrome b-cl segment.