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Reversible redox energy coupling in electron transfer chains
Reversibility is a common theme in respiratory and photosynthetic systems that couple electron transfer with a transmembrane proton gradient driving ATP production. This includes the intenselyExpand
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Back‐reactions, short‐circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O2
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: withExpand
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Exposing the complex III Qo semiquinone radical.
Complex III Qo site semiquinone has been assigned pivotal roles in productive energy-conversion and destructive superoxide generation. After a 30-year search, a genetic heme bH knockout arrests thisExpand
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Fixing the Q cycle.
Mitchell's key insight that all bioenergetic membranes run on the conversion of redox energy into transmembrane electrical and proton gradients took the form 30 years ago of a working model of the QExpand
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An Electronic Bus Bar Lies in the Core of Cytochrome bc1
Heme Communication Revealed by Asymmetry An electronic bus bar is an electrical conductor that connects several circuits. Świerczek et al. (p. 451) now find that a similar strategy is used by theExpand
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Discrimination between two possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc1
In addition to its bioenergetic function of building up proton motive force, cytochrome bc1 can be a source of superoxide. One-electron reduction of oxygen is believed to occur from semiquinone (SQo)Expand
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Demonstration of Short-lived Complexes of Cytochrome c with Cytochrome bc1 by EPR Spectroscopy
One of the steps of a common pathway for biological energy conversion involves electron transfer between cytochrome c and cytochrome bc1. To clarify the mechanism of this reaction, we examined theExpand
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Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center mapped by site-directed mutagenesis.
The crystallographic structure of the Blastochloris (formerly called Rhodopseudomonas) viridis tetraheme cytochrome subunit bound to the photosynthetic reaction center (RC) suggests that all fourExpand
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Interaction site for high-potential iron-sulfur protein on the tetraheme cytochrome subunit bound to the photosynthetic reaction center of Rubrivivax gelatinosus.
We have recently demonstrated, using site-directed mutagenesis, that soluble cytochromes interact with the Rubrivivax gelatinosus photosynthetic reaction center (RC) in the vicinity of theExpand
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Parameterization of the prosthetic redox centers of the bacterial cytochrome bc1 complex for atomistic molecular dynamics simulations
Cytochrome (cyt) bc1 is a multi-subunit membrane protein complex that is a vital component of the respiratory and photosynthetic electron transfer chains both in bacteria and eukaryotes. Although theExpand
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