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Resonance condition cytochrome

No overtones or combinations involving more than two quanta are observed, which is consistent with the absence of a 0-2 transition in absorption. The second-order bands in the resonance Raman spectrum of cytochrome c are shown in Fig. 20 (Section 4.8) where they appear in the 1650-3 300 cm region for excitation at 514.5 nm (point F). The excitation profiles of the second-order bands should peak only in the 0-1 absorption region, at positions consistent with the wavenumbers of the relevant fundamentals. This behaviour is expected since the appropriate parts of the scattering tensor show only 0—1 resonance conditions ... [Pg.32]

Perhaps the most important application of resonance Raman spectroscopy has been to the study ol biological molecules under physiologically significant conditions that is. in the presence of water and at low to moderate concentration levels.. - s an example, the technique has been useil lo determine the oxidation state and spin of iron atoms in hemoglobin and cytochrome c. In these molecules, the lesonance Raman bands are due solelv to ibrational modes of the tetra-... [Pg.494]

In this contribution, we extend previous resonance Raman investigations of the Dl-D2-cytochrome bggg complex (3,4,5). Structural features of chlorophylls bound to Dl-D2-cytochrome bjs complexes and the chlorophyll-containing 47 kDa protein are determined by using both resonance and nearresonance conditions. [Pg.643]


See other pages where Resonance condition cytochrome is mentioned: [Pg.114]    [Pg.691]    [Pg.391]    [Pg.288]    [Pg.310]    [Pg.288]    [Pg.374]    [Pg.587]    [Pg.477]    [Pg.30]    [Pg.31]    [Pg.92]    [Pg.354]   
See also in sourсe #XX -- [ Pg.92 ]




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