The structural bases for the unique ligand binding properties of Glycera dibranchiata hemoglobins. A resonance Raman study.
作者： M R Ondrias , S D Carson , I Constantinidis , J Mintorovitch , J D Satterlee
DOI: 10.1016/S0021-9258(17)35925-2
关键词: Myoglobin 、 Porphyrin 、 Heme 、 Ligand (biochemistry) 、 Protein quaternary structure 、 Resonance Raman spectroscopy 、 Stereochemistry 、 Chemistry 、 Histidine 、 Protein structure
摘要: The hemoglobin of the marine annelid Glycera dibranchiata possesses several unique features: consists multiple monomeric and polymeric components, quaternary structure is lacking, distal histidine replaced by leucine in at least one constituent, 4) protein exhibits extremely rapid ligand binding kinetics. effect these structural modifications on process has been evaluated using resonance Raman spectroscopy to examine vibrational modes porphyrin macrocycle deoxy carbonmonoxy equilibrium species G. both unseparated forms a single component designated Fraction II. Significant differences relative were found pi electron density, vinyl environment, low frequency modes, and, particular, Fe-proximal stretching mode. Spectra heme transients generated within 10 ns photolysis have also examined. These clearly indicate large pocket dynamics subsequent CO hemoglobins other hemoglobins. significance results terms kinetics thermodynamics discussed.
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