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Myoglobin, absorption spectrum structure

Hb possesses both 4 and 5-coordinate forms as demonstrated by the Raman spectra (Figure 1) and the spj it Soret band of the absorption spectrum (9,36). In contrast, Mb shows only the red Soret component and the Raman lines characteristic of the 5-coordinate form. Thus, myoglobin s R-like structure favors the 5-coordinate form. The R/T difference in affinity for histidine might also be expected to reveal itself in the strength of the Ni-histidine bond. In native Fe hemoglobin, the Fe-histidine bond increases in strength upon conversion from the T to R structure (31,39). [Pg.237]


See other pages where Myoglobin, absorption spectrum structure is mentioned: [Pg.455]    [Pg.82]    [Pg.281]    [Pg.320]    [Pg.21]    [Pg.381]    [Pg.372]    [Pg.372]    [Pg.451]    [Pg.214]    [Pg.38]    [Pg.216]    [Pg.973]    [Pg.1079]    [Pg.145]   
See also in sourсe #XX -- [ Pg.477 ]




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