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Nature of biological electron transfer
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.
Natural engineering principles of electron tunnelling in biological oxidation–reduction
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.
Reversible redox energy coupling in electron transfer chains
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.
Engineering protein structure for electron transfer function in photosynthetic reaction centers.
Biological electron transfer
- C. Moser, C. C. Page, R. Farid, P. Dutton
- PhysicsJournal of bioenergetics and biomembranes
- 1 June 1995
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.
Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems.
- P. Dutton
- ChemistryMethods in enzymology
P450 BM3: the very model of a modern flavocytochrome.
Fixing the Q cycle.
Mechanism for electron transfer within and between proteins.