This is an overview of some of the important, challenging, and problematic issues in contemporary electron transfer research. After a qualitative discussion of electron transfer, its time and distance scales, energy curves, and basic parabolic energy models are introduced to define the electron transfer process. Application of transition state theory leads to the standard Marcus formulation of electron transfer rate constants. Electron transfer in solution is coupled to solvent polarization effects, and relaxation processes can contribute to and even control electron transfer. The inverted region, in which electron transfer rate constants decrease with increasing exoergicity, is one of the most striking phenomena in electron transfer chemistry. It is predicted by both semiclassical and quantum mechanical models, with the latter appropriate if there are coupled high- or medium-frequency vibrations. The intramolecular reorganizational energy has different contributions from different vibrational modes, whic...

Contemporary Issues in Electron Transfer Research

Electron Transfer Past and Future (R Marcus) Electron Transfer Reactions in Solution: A Historical Perspective (N Sutin) Electron Transfer--From Isolated Molecules to Biomolecules (M Bixon & J Jortner) Charge Transfer in Bichromophoric Molecules in the Gas Phase (D Levy) Long--Range Charge Separation in Solvent--Free Donor--Bridge--Acceptor Systems (B Wegewijs & J Verhoeven) Electron Transfer and Charge Separation in Clusters (C Dessent, et al) Control of Electron Transfer Kinetics: Models for Medium Reorganization and Donor--Acceptor Coupling (M Newton) Theories of Structure--Function Relationships for Bridge--Mediated Electron Transfer Reactions (S Skourtis & D Beratan) Fluctuations and Coherence in Long--Range and Multicenter Electron Transfer (G Iversen, et al) Lanczos Algorithm for Electron Transfer Rates in Solvents with Complex Spectral Densities (A Okada, et al) Spectroscopic Determination of Electron Transfer Barriers and Rate Constants (K Omberg, et al) Photoinduced Electron Transfer Within Donor--Spacer--Acceptor Molecular Assemblies Studied by Time--Resolved Microwave Conductivity (J Warman, et al) From Close Contact to Long--Range Intramolecular Electron Transfer (J Verhoeven) Photoinduced Electron Transfers Through sigma Bonds in Solution (N--C Yang, et al) Indexes

Electron transfer : from isolated molecules to biomolecules

Primary and secondary protium-to-tritium (H/T) and deuterium-to-tritium (D/T) kinetic isotope effects for the catalytic oxidation of benzyl alcohol to benzaldehyde by yeast alcohol dehydrogenase (YADH) at 25 degrees Celsius have been determined. Previous studies showed that this reaction is nearly or fully rate limited by the hydrogen-transfer step. Semiclassical mass considerations that do not include tunneling effects would predict that kH/kT = (kD/kT)3.26, where kH, kD, and kT are the rate constants for the reaction of protium, deuterium, and tritium derivatives, respectively. Significant deviations from this relation have now been observed for both primary and especially secondary effects, such that experimental H/T ratios are much greater than those calculated from the above expression. These deviations also hold in the temperature range from 0 to 40 degrees Celsius. Such deviations were previously predicted to result from a reaction coordinate containing a significant contribution from hydrogen tunneling.

https://science.sciencemag.org/content/sci/243/4896/1325.full.pdf

Hydrogen tunneling in enzyme reactions

Phthalate dioxygenase reductase (PDR) is a prototypical iron-sulfur flavoprotein (36 kilodaltons) that utilizes flavin mononucleotide (FMN) to mediate electron transfer from the two-electron donor, reduced nicotinamide adenine nucleotide (NADH), to the one-electron acceptor, [2Fe-2S]. The crystal structure of oxidized PDR from Pseudomonas cepacia has been analyzed at 2.0 angstrom resolution resolution; reduced PDR and pyridine nucleotide complexes have been analyzed at 2.7 angstrom resolution. NADH, FMN, and the [2Fe-2S] cluster, bound to distinct domains, are brought together near a central cleft in the molecule, with only 4.9 angstroms separating the flavin 8-methyl and a cysteine sulfur ligated to iron. The domains that bind FMN and [2Fe-2S] are packed so that the flavin ring and the plane of the [2Fe-2S] core are approximately perpendicular. The [2Fe-2S] group is bound by four cysteines in a site resembling that in plant ferredoxins, but its redox potential (-174 millivolts at pH 7.0) is much higher than the potentials of plant ferredoxins. Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP(+)-reductase.

https://science.sciencemag.org/content/sci/258/5088/1604.full.pdf

Phthalate Dioxygenase Reductase: A Modular Structure for Electron Transfer from Pyridine Nucleotides to [2Fe-2S]

The connections between basic electron transfer theory and the methods currently available for analyzing quantum electronic interactions of long-range electron transfer within and between proteins are examined. Both traditional basis set expansion as well as quantum path integral Monte Carlo descriptions of propagation through the intervening medium are described and compared. The development of the concepts and technical aspects of superexchange are traced from simple to complex implementations, with an emphasis on the unifying framework of the sum over tunnelling path amplitudes. Directions for the future refinement of quantitative biomolecular computations are identified.

https://science.sciencemag.org/content/sci/236/4809/1647.full.pdf

Electron tunneling paths in proteins.

An experimental investigation of the distance dependence of long-range electron transfer in zinc/ruthenium-modified myoglobins has been performed. The modified proteins were prepared by substitution of zinc mesoporphyrin IX diacid (ZnP) for the heme in each of four previously characterized pentaammineruthenium(III) (a_5Ru;a = NH_3) derivatives of sperm whale myoglobin (Mb): a_5Ru(His-48)Mb, a_5Ru(His-12)Mb, a_5Ru(His-116)Mb, a_5Ru(His-81)Mb. Electron transfer from the ZnP triplet excited state (^3ZnP*) to Ru^3+, ^3ZnP*-Ru^3+ → ZnP^+-Ru^2+ (ΔE° ~ 0.8V) was measured by time-resolved transient absorption spectroscopy: rate constants (k_f) are 7.0 × 10^4 (His-48), 1.0 × 10^2 (His-12), 8.9 × 10^1 (His-116), and 8.5 × 10^1 (His-81) s^-1 at 25 °C. Activation enthalpies calculated from the temperature dependences of the electron-transfer rates over the range 5-40 °C are 1.7 ± 1.6 (His-48), 4.7 ± 0.9 (His-12), 5.4 ± 0.4 (His-116), and 5.6 ± 2.5 (His-81) kcal mol^-1. Electron-transfer distances (d = closest ZnP edge to a_5Ru(His) edge; angstroms) were calculated to fall in the following ranges: His-48, 11.8-16.6; His-12, 21.5-22.3; His-116, 19.8-20.4; His-81, 18.8-19.3. The rate-distance equation is k_f = 7.8 × 10^8 exp[-0.9l(d - 3)] s^-1 . The data indicate that the ^3ZnP*-Ru(His-12)^3+ electronic coupling may be enhanced by an intervening tryptophan (Trp-14).

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Distance dependence of photoinduced long-range electron transfer in zinc/ruthenium-modified myoglobins

Franck-Condon analyses on the IBM PC/AT

Long-range-electron transfer (ET) reactions are important mechanistic steps in many biological processes1 Current research in this area has focused on elucidating the factors that control these ET processes in donor-acceptor (D-A) systems2–9 A general two-site model consists of a donor (D) and acceptor (A) that are fixed in a rigid structure (eg, protein matrix) and separated by a through-space distance, d Donor to acceptor ET pathways through chemical bonds are also possible, but generally are longer than the through-space distance

Michael Albin

Papers

Distance dependence of photoinduced long-range electron transfer in zinc/ruthenium-modified myoglobins

Franck-Condon analyses on the IBM PC/AT

Long-Range Electron Transfer in Ruthenium-Modified Proteins

Multi-variant kinetic analyses on a microcomputer