Electron transfer reaction, conformational control

The mechanism of the regulation of electron transfer in metalloproteins has been investigated 61) and two relevant examples have been discussed in the first one the molecular mechanism controlling the electron transfer reactions is restricted to the immediate chemical environment of the metal center (azurin), while in the second one it involves a conformational transition of the whole quaternary structure of the enzyme. The power of the kinetic approach in detecting significant intermediates was emphasized 6t>. The Cu metal complex site of azurin has a distorted tetrahedral... 

Hammes-Schiffer S. Theoretical perspectives on proton-coupled electron transfer reactions. Acc. Chem. Res. 2001 34 273-281. Khoshtariya DE, Wei J, Liu H, Yue H, Waldeck DH. Charge-transfer mechanism for cytochrome c adsorbed on nanometer thick films, distinguishing frictional control from conformational gating. J. Am. Chem. Soc. 2003 125 7704-7714. 

The Marcus Theory can also be applied for heterogeneous electron transfer reaction at electrode surfaces [24 and references therein]. The electronic coupling between the protein and the electrode can be varied using different self-assembled monolayers controlling the orientation of the redox active protein on the surface and the distance between the redox active site of the protein and the electrode. The driving force is related to the appHed potential and the redox potential of the protein. In many cases the rate of electron transfer across the protein-electrode interface is limited by conformational reorganization. This has focussed the efforts of many groups on tailored interaction between proteins and enzymes and electrode surfaces. 

Theoretical models available in the literature consider the electron loss, the counter-ion diffusion, or the nucleation process as the rate-limiting steps they follow traditional electrochemical models and avoid any structural treatment of the electrode. Our approach relies on the electro-chemically stimulated conformational relaxation control of the process. Although these conformational movements179 are present at any moment of the oxidation process (as proved by the experimental determination of the volume change or the continuous movements of artificial muscles), in order to be able to quantify them, we need to isolate them from either the electrons transfers, the counter-ion diffusion, or the solvent interchange we need electrochemical experiments in which the kinetics are under conformational relaxation control. Once the electrochemistry of these structural effects is quantified, we can again include the other components of the electrochemical reaction to obtain a complete description of electrochemical oxidation. 

Mattay et al. examined the regioselective and stereoselective cyclization of unsaturated silyl enol ethers by photoinduced electron transfer using DCA and DCN as sensitizers. Thereby the regiochemistry (6-endo versus 5-exo) of the cyclization could be controlled because in the absence of a nucleophile, like an alcohol, the cyclization of the siloxy radical cation is dominant, whereas the presence of a nucleophile favors the reaction pathway via the corresponding a-keto radical. The resulting stereoselective cis ring juncture is due to a favored reactive chair like conformer with the substituents pseudoaxial arranged (Scheme 27) [36,37]. 

Electron transfer from the substrates to 02 proceeds by a redox cycle that consists of copper(II) and copper(I). The high catalytic activity of the copper complex can be explained as follows (1) The redox potential of Cu(I)/Cu(II) fits the redox reaction. (2) The high affinity of Cu(I) to 02 results in rapid reoxidation of the catalyst. (3) Monomers can coordinate to, and dissociate from, the copper complex, and inner-sphere electron transfer proceeds in the intermediate complex. (4) The complex remains stable in the reaction system. It may be possible to investigate other catalysts whose redox potentials can be controlled by the selection of ligands and metal species to conform with these requisites several other suitable catalysts for oxidative polymerization of phenols, such as manganese and iron complexes, are candidates on the basis of their redox potentials. 

The electron transfer mechanism of azurin, a well known example for this type of proteins, has been systematically studied using the chemical relaxation method and a well defined inorganic outer sphere redox couple. In parallel, the investigations of the reaction with its presumed physiological partner, cytochrome c, were pursued (7). The specificity of the interaction between azurin and cytochrome c P-551 is expressed in higher specific rates and in the control of the electron transfer equilibrium by conformational transitions of both proteins. 

The first experimental evidences that electron transfer from QA to P+ and from QA to Qb in reaction centers are controlled by the protein conformational dynamics, was obtained in the late 1970 s (Berg 1978a,b Likhtenshtein et al., 1979 a, b) This conclusion was confirmed in subsequent experimental studies in which molecular dynamics of RC and the photsynthetic membrane were determined with a whole set of physical labels. (Kotelnikov et al., 1983, Kochetkov et al., 1984 Parak et al., 1983). It was shown that the electron transfer from reduced primary acceptor QA to secondary acceptor Qb takes place only under conditions in which the labels record the mobility of the protein moiety in the membrane with the correlation frequency u0 > 107 s-1 (Fig. 3.16). 

In a few systems, quenching rate constants tend toward saturation below the diffusion-controlled limit . This may be observed when the quenching reaction does not involve an electron-transfer process (e.g. , [ RuL3] -[Cr )] ), when the electron transfer is highly nonadiabatic, when the reactive form of the quencher is not the dominant form in solution (e.g. , [ RuL3] -[CU( )] , or when a substitutional or conformational change becomes rate determining. ... 

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