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J. Biol. Chem., Vol. 262, Issue 31, 14885-14890, 11, 1987

Ligand binding channels reflected in the resonance Raman spectra of cryogenically trapped species of myoglobin

BF Campbell, MR Chance and JM Friedman
AT&T Bell Laboratories, Murray Hill, New Jersey 07974.

Variations in the v2 region of the Raman spectra of cryogenically trapped photoproducts of different liganded myoglobins as a function of ligand (CO, O2, and n-butyl isocyanide) and species (whale, tuna, elephant) are reported. These variations are attributed to differences in the population of "open" (ligand accessible) and "closed" (ligand inaccessible) conformations of the distal heme pocket. Based on these findings and those derived from other spectroscopies including x-ray crystallography, NMR, IR spectra, and ESR, a working model is presented which accounts for how the conformation of the distal heme pocket, the geometry of the bound ligand, the identity of the ligand, and the dynamics of the dissociated ligand are all interconnected.
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