Mechanism of T1 relaxation in 13CO complexed to an iron porphyrin: implications for CO bonding in heme proteins

Autor:	J. D. Satterlee, T. Perkins, J. H. Richards
Rok vydání:	1983
Předmět:	Hemeprotein Chemistry Chemical shift Spin–lattice relaxation General Chemistry Biochemistry Porphyrin Catalysis Crystallography chemistry.chemical_compound Colloid and Surface Chemistry Monomer Relaxation (physics) Hemoglobin Hemin
Zdroj:	Journal of the American Chemical Society. 105:1350-1354
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja00343a047
Popis:	Chemical shifts and spin-lattice relaxation parameters for ^(13)CO bonded to the complex 1 -methylimidazole-iron protoporphyrin dimethyl ester are reported. The ^(13)CO chemical shifts are much different from those observed in the carbonyl vertebrate hemoglobins, but remarkably similar to that observed for the monomeric hemoglobin component from Glycera dibranchiata. The relaxation parameter, T_1, is shown to change dramatically upon ligation to both the hemin model system and to hemoglobin A. The mechanisms of spin-lattice relaxation are dominated by chemical shift anisotropy for ^(13)CO bound to both hemins and proteins, but, in the latter, dipole-dipole forces make an additional contribution to the overall relaxation rate.
Databáze:	OpenAIRE
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