Proton-coupled electron transfer (PCET) is an important mechanism for charge transfer in a wide variety of systems including biology- and materials-oriented venues. We review several areas where the transfer of an electron and proton is tightly coupled and discuss model systems that can provide an experimental basis for a test of PCET theory. In a PCET reaction, the electron and proton may tran...

In cytochrome c oxidase, a requirement for proton pumping is a tight coupling between electron and proton transfer, which could be accomplished if internal electron-transfer rates were controlled by uptake of protons. During reaction of the fully reduced enzyme with oxygen, concomitant with the "peroxy" to "oxoferryl" transition, internal transfer of the fourth electron from CuA to heme a has t...

A molecular theory of the dynamic solvent effects on an outer-sphere adiabatic electron transfer reaction is presented. The theory properly includes the role of the microscopic correlations present in a dense dipolar solvent in the dynamics of an electron-transfer reaction. The theory predicts that the translational modes of the solvent, hitherto neglected in most discussions on electron-transf...

Electron transfer within rat neuronal nitric-oxide synthase (nNOS) was investigated by pulse radiolysis. Radiolytically generated 1-methyl-3-carbamoyl pyridinium (MCP) radical was found to react predominantly with the heme of the enzyme with a second-order rate constant for heme reduction of 3 x 10(8) m(-1) s(-1). In the calmodulin (CaM)-bound enzyme a subsequent first-order phase was observed ...

The ability of Geobacter sulfurreducens to utilize electrodes as electron acceptors provides a system for monitoring mechanisms of electron transfer beyond the cell surface. This study examined the physiology of extracellular electron transfer during many stages of growth, and in response to shortand long-term changes in electron acceptor potential. When G. sulfurreducens was grown on planar po...

Electron transfer from the Rieske iron-sulfur protein to cytochrome c(1) (cyt c(1)) in the Rhodobacter sphaeroides cytochrome bc(1) complex was studied using a ruthenium dimer complex, Ru(2)D. Laser flash photolysis of a solution containing reduced cyt bc(1), Ru(2)D, and a sacrificial electron acceptor results in oxidation of cyt c(1) within 1 micros, followed by electron transfer from the iron...

The bacterial reaction center couples light-induced electron transfer to proton pumping across the membrane by reactions of a quinone molecule Q(B) that binds two electrons and two protons at the active site. This article reviews recent experimental work on the mechanism of the proton-coupled electron transfer and the pathways for proton transfer to the Q(B) site. The mechanism of the first ele...

Interprotein electron transfer plays an important role in biological energy conversion. In this work, the electron transfer reaction between cytochrome c(2) (cyt) and the reaction center (RC) was studied to determine the mechanisms coupling association and electron transfer. Previous studies have shown that mutation of hydrophobic residues in the reaction interface, particularly Tyr L162, chang...

1H NMR line broadening measurements show that the electron self-exchange rate constant for ((trimethylamino)methyl)ferrocenium/ferrocene (TMAFc(2+/+)) in D(2)O as solvent is decreased by ca. 20-50 fold in the presence of excess beta-cyclodextrin. The rate effect is associated with the selective hydrophobic encapsulation of the ferrocene form of the redox couple (i.e., the ferrocenium form is no...

Electron-transfer cross-reactions between neutral molecules and their radical cations spanning a wide range of structural type and intrinsic reactivity have been analyzed using classical Marcus theory. The principal factor found to govern intrinsic reactivity is the inner-shell bond reorganization energy. The HOMO-LUMO overlap of alkyl groups on reacting molecules is generally sufficient to pro...