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Nature of biological electron transfer

TLDR
Powerful first-order analysis of intraprotein electron transfer is developed from electron-transfer measurements both in biological and in chemical systems, finding selection of distance, free energy and reorganization energy are sufficient to define rate and directional specificity of biological electron transfer.
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Natural engineering principles of electron tunnelling in biological oxidation–reduction

TLDR
The 14 Å or less spacing of redox centres provides highly robust engineering for electron transfer, and may reflect selection against designs that have proved more vulnerable to mutations during the course of evolution.
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Reversible redox energy coupling in electron transfer chains

TLDR
This work progressively inactivated individual cofactors comprising cytochrome bc1, and resolved millisecond reversibility in all electron-tunnelling steps and coupled proton exchanges, including charge-separating hydroquinone–quinone catalysis at the Qo site, which shows that redox equilibria are relevant on a catalytic timescale.
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Engineering protein structure for electron transfer function in photosynthetic reaction centers.

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Biological electron transfer

TLDR
New results from the photosynthetic reaction center protein confirm that the electronic-tunneling medium appears relatively homogeneous, with any variances evident having no impact on function, and that control of intraprotein rates and directional specificity rests on a combination of distance, free energy, and reorganization energy.
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Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems.

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P450 BM3: the very model of a modern flavocytochrome.

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Fixing the Q cycle.

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Mechanism for electron transfer within and between proteins.

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Electron tunneling chains of mitochondria.

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