Titlebook: Charge and Field Effects in Biosystems—3; Milton J. Allen,Stephen F. Cleary,Donald D. Shilla Book 1992 Birkhäuser Boston 1992 ELF.X-ray.el

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Fresh Approaches and New Surprises with Iron-Sulfur Clusterset al. 1985), or by exogenous ligands. The latter case is exemplified by aconitase in which one Fe subsite of the [4Fe-4S] core is not ligated by cysteine but by OH- (Robbins and Stout, 1989; Werst et al., 1990). This coordinatively differentiated Fe also binds the organic substrates (Beinert and Ke

Chivalrous

The Direct Electron Transfer Reactions of Cytochrome Oxidase Immobilized into a Membrane Modified Elt that heterogeneous catalytic communication between cytochrome c oxidase on the electrode is occurring with its solution resident biological redox partner, reduced cytochrome c. The homogeneous electron transfer reaction between cytochrome c and cytochrome oxidase had been studied earlier (Long et

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Selection Rules on Helicity during Discrete Transitions of the Genome Conformational State in Intacts effectiveness lies between the two circular polarizations. Conversely, left-handed polarized EHF EMR is effective when x-rayed cells are exposed to microwaves at the resonant frequency of the first resonance (41.32 GHz). It was shown that the difference in the effectiveness of the two circularly p

Water-Brash

Charge Transfer Effect on Coelomic Cells in Exalted Bioluminescence of ,ents to identify the electroactive components of the cell that are linked to the production of the active ingredients. As the synthesis of luciferin and luciferase are genetic (we do know that out of the 33 genera of earthworms only 16 of them are bioluminescent), specific directions for the amino a

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Cougar

https://doi.org/10.1007/978-3-211-38365-0e that Fe-S clusters have important functions outside the realm of one-electron transfer (Beinert,1989). One particularly exciting development has been the discovery of Lewis acid catalytic activity in aconitase (Beinert, 1989; Beinert and Kennedy, 1989) and most recently, there is evidence to sugge

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https://doi.org/10.1007/978-3-211-38365-0s (e.g., Swalen et al.,1987; Chidsey and Loiacono, 1990). Some of this research has been directed toward a biochemical approach (Hafeman et al., 1981; Ishiguro and Nakanishi, 1984; Brian and McConnell, 1984; Fabianowski et al., 1989; Prime and Whitesides, 1991; Tarlov and Bowden, 1991). In this pape

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https://doi.org/10.1007/978-3-211-38365-0 is the ability of heme proteins to serve as electron carriers. The heme group, an iron atom bound to the four nitrogens of a porphyrin ring system, is the characteristic structural feature in common to all heme proteins. The iron atom serves as the site of oxidation or reduction during electron tra

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