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Cytochrome reorientation

In the first area we have gone a step backward recently in order to make two steps forward. The reduced tuna cytochrome map at 2 A resolution is in good shape, the oxidized horse cytochrome map at 2.8 A is of poor quality, and the oxidized tuna map at 2 A that will replace it is completed but not interpreted at the time of writing. The opening of the heme crevice at phenylalanine-82 in the oxidized state that was reported from the horse map (12) apparently is not correct, and any comments about the finer reorientations of aromatic or other side chains must wait for confirmation from the new tuna map. Much can be said now about areas 2 through 5 above, however, to lay the groundwork for a later discussion of the first area. [Pg.464]

Kupfer, R., S.Y. Liu, A.J. Allentoff, and J.A. Thompson (2001). Comparisons of hydroperoxide isomerase and monooxygenase activities of cytochrome P450 for conversions of allylic hydroperoxides and alcohols to epoxyalcohols and diols Probing substrate reorientation in the active site. Biochemistry 40, 11490-11501. [Pg.36]

The tin oxide/cytochrome c interface is quite complex and there are alternatives to adsorbate reorientation which could also conceivably account for the observed dependence of ket on scan rate. The changing potential which occurs during the CV scan could result in chemical changes to the tin oxide itself or could induce conformational changes or slight denaturation in the adsorbed cytochrome c molecules. An alternative with a non-dynamic origin is an equilibrium distribution of electron... [Pg.71]

Cytochrome c can be strongly adsorbed in its native state on tin oxide electrodes at coverages of several tenths of a monolayer. Measurements of unimolecular electron transfer rate constants for adsorbed cytochrome c can be readily made in the absence of solution cytochrome c using cyclic voltammetry. The kinetic results are consistent with an interfacial model involving electrostatic interaction between the tin oxide and the exposed heme edge of the cytochrome as well as an electrostatically driven adsorbate reorientation capability to account for the anomalous dependence of rate constant on scan rate. Other possible explanations for the... [Pg.73]


See other pages where Cytochrome reorientation is mentioned: [Pg.159]    [Pg.414]    [Pg.416]    [Pg.934]    [Pg.184]    [Pg.79]    [Pg.796]    [Pg.479]    [Pg.934]    [Pg.129]    [Pg.165]    [Pg.53]    [Pg.159]    [Pg.12]    [Pg.353]    [Pg.4554]    [Pg.5895]    [Pg.71]    [Pg.71]   
See also in sourсe #XX -- [ Pg.7 , Pg.644 ]




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