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Binding favorable

Goethite EXAFS study of As(V) and Cr(VI) adsorption on goethite. Monodentate binding favored at low surface coverage of As(V), bidentate at high surface coverage Fendorf et al. (1997)... [Pg.308]

Franke A, Jung C, Stochel G, van Eldik R. Substrate binding favors enhanced NO binding to P450cam. J Am Chem Soc 2004 126 4181-91. [Pg.325]

Critically important as well in determining the binding mode is the chirality of the metal complex.Intercalation into the right-handed helix favors the A-isomer, whereas groove binding favors the A-isomer. Figure 8.7 illustrates these symmetry-selective interactions. In intercalation, we consider that one phenan-... [Pg.468]

Fig. 2.6 A cartoon representation of a model for POR-P450 complex formation in the endoplasmie reticulum (ER) membrane. Flavin mononucleotide (FMN) domain, flavin adenine dinueleotide FAD) domain, and P450s are shown in blue, yellow, and red balls, respeetively. (1) Multiple P450s exist in the ER membrane. Nucleotide binding favors formation of the elosed form, similar to the one found in the erystal strueture [36]. (2) Upon binding to pyridine nueleotide (NADPH), the enzyme adopts the elosed form. In the elosed form, hydride transfer, inter-... Fig. 2.6 A cartoon representation of a model for POR-P450 complex formation in the endoplasmie reticulum (ER) membrane. Flavin mononucleotide (FMN) domain, flavin adenine dinueleotide FAD) domain, and P450s are shown in blue, yellow, and red balls, respeetively. (1) Multiple P450s exist in the ER membrane. Nucleotide binding favors formation of the elosed form, similar to the one found in the erystal strueture [36]. (2) Upon binding to pyridine nueleotide (NADPH), the enzyme adopts the elosed form. In the elosed form, hydride transfer, inter-...

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See also in sourсe #XX -- [ Pg.157 ]




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Favorable binding sites, GRID

Favored

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