Engineering electron transfer

Moser, C.C., Dutton, P.L. Biological electron transfer measurement, mechanism, engineering requirements. In Quantum mechanical simulation methods for studying biological systems, D. Bicout and M. Field, eds. Springer, Berlin (1996) 201-214. 

Mauk AG (1991) Electron Transfer in Genetically Engineered Proteins. The Cytochrome c Paradigm.75 131-158... 

Okuda J, Yamazaki T, Fukasawa M, Kakehi N, Sode K. 2007. The application of engineered glucose dehydrogenase to a direct electron-transfer-type continuous glucose monitoring system and a compartmentless biofuel cell. Anal Lett 40 431 -440. 

Molecular engineering of ruthenium complexes that can act as panchromatic CT sensitizers for Ti02-based solar cells presents a challenging task as several requirements have to be fulfilled by the dye, which are very difficult to be met simultaneously. The lowest unoccupied molecular orbitals (LUMOs) and the highest occupied molecular orbitals (HOMOs) have to be maintained at levels where photo-induced electron transfer into the Ti02 conduction band and regeneration... 

Figure 6.14 Cyclic voltammogram obtained for a multiple-electron-transfer system, where a thin film of sputtered V2O5 on a platinum working electrode has been immersed in an electrolyte solution of propylene carbonate containing LiCI04 (1.0 mol dm ). From Cogan, S. F., Nguyen, N. M Perrotti, S. J. and Rauh, R. D Electroctromism in sputtered vanadium pentoxide , SPIE, 1016, 57-62 (1989). Reproduced by permission of the International Society for Optical Engineering (SPIE).

Utilization of a domain linker to control electron flow is not unique to NOS. Like NOS, P450BM-3 has the heme and reductase domains fused to give a heme-FMN-FAD architecture (75). In addition, the linker between the heme and FMN domains is critical for electron transfer. Engineering studies on the P450BM-3 linker reveals that the length of the linker but not the sequence is critical in controlling the FMN-to-heme electron transfer reaction 135,136). Similar experiments with flavocy-tochrome b2 137) illustrate the importance of the linker in interdomain electron transfer, presumably by assisting in proper orientation of redox partners. The same appears to be true for NOS, with the important... 

Although NOS is a dimer, it is reasonable to assume that electron transfer is confined to intrapolypeptide electron transfer within one subunit. However, some clever engineering studies indicate that this may not the case, and that the reductase of one subunit is the electron donor to the neighboring subimit (139) (Fig. 13). This should provide some limitation on the possible models that can be proposed based on current structural information, including the estimated distance between FMN and heme as > 15 A (140). At least two quite different sites have been proposed for docking of the reductase domain (80, 81), each with its own attractive features, although neither has as yet been directly tested by suitably designed experiments. Another puzzle with respect to electron transfer is the requirement for three electrons to... 

Given that interfacial solvation affects chemical transport/ surface reactivity and electron transfer/ and macromolecular self-assembly/ predictive models of solvent-solute interactions near surfaces will afford researchers deeper insights into a host of phenomena in biology, physics, and engineering. Research in this area should aid efforts to develop a general, experimentally tested, and quantitative understanding of solution-phase surface chemistry. 

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