Resonance effects in strongly exothermic long‐range electron transfer and their possible implications for the behaviour of site‐directed mutant proteins
Open Access
- 16 January 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 296 (2) , 141-144
- https://doi.org/10.1016/0014-5793(92)80365-n
Abstract
Long‐range electron transfer investigations of hemoproteins, blue copper and iron‐sulphur proteins frequently rest on electronically excited metall centres. When the excitation energy approaches the oxidation or reduction potentials of intermediate residues the superexchange view normally used, however, fails and a variety of new dynamic features arise. These all involve population of the intermediate cation or anion residue states which can be partially or wholly vibrationally relaxed. We discuss suitable views and a new theoretical formalism for these phenomena. We also note some important implication for site‐directed mutagenesis in long‐range, strongly exothermic electron transfer processes.Keywords
This publication has 28 references indexed in Scilit:
- Preparation, characterization, and intramolecular electron transfer in pentaammineruthenium histidine-26 cytochrome b5 derivatives: role of the intervening medium in long-range donor-acceptor electronic couplingJournal of the American Chemical Society, 1991
- Reorganization Energies for Protein-to-Protein Electron Transfer and Interfacial Dynamics: “Playing Fast and Loose”Molecular Crystals and Liquid Crystals, 1991
- Long Range Electron Transfer in Blue Copper ProteinsMolecular Crystals and Liquid Crystals, 1991
- Long-range electron transfer in a cytochrome c derivative containing a covalently attached cobalt cage complexJournal of the American Chemical Society, 1989
- Preparation and characterization of two His-59 ruthenium-modified algal plastocyanins and an unusually small rate constant for ruthenium(II) .fwdarw. copper(II) intramolecular electron transfer over.apprx.12 .ANG.Journal of the American Chemical Society, 1988
- Long-distance electron transfer in proteins and model systemsAccounts of Chemical Research, 1988
- Distance dependence of photoinduced long-range electron transfer in zinc/ruthenium-modified myoglobinsJournal of the American Chemical Society, 1988
- Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants.Proceedings of the National Academy of Sciences, 1987
- Temperature dependence of and ligation effects on long-range electron transfer in complementary (zinc,ferric) hemoglobin hybridsJournal of the American Chemical Society, 1986
- Preparation and characterization of pentaammineruthenium-(histidine-83)azurin: thermodynamics of intramolecular electron transfer from ruthenium to copper.Proceedings of the National Academy of Sciences, 1984