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

B. F. Campbell, M. R. Chance, Joel M. Friedman

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)14885-14890
Number of pages6
JournalJournal of Biological Chemistry
Volume262
Issue number31
StatePublished - Nov 5 1987
Externally publishedYes

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Myoglobin
Raman scattering
Ligands
Heme
Conformations
Whales
Tuna
Crystallography
Carbon Monoxide
Paramagnetic resonance
Spectrum Analysis
Nuclear magnetic resonance
X-Rays
Spectroscopy
X rays
Geometry
Population

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ligand binding channels reflected in the resonance Raman spectra of cryogenically trapped species of myoglobin. / Campbell, B. F.; Chance, M. R.; Friedman, Joel M.

In: Journal of Biological Chemistry, Vol. 262, No. 31, 05.11.1987, p. 14885-14890.

Research output: Contribution to journalArticle

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