Multinuclear (13C, 17O, 57Fe) NMR studies of carbonmonoxy heme proteins and synthetic model compounds.

摘要: Abstract 13 C, 17 O and 57 Fe NMR spectra of several carbonmonoxy hemoprotein models with varying polar steric effects the distal organic superstructure, constraints proximal side, porphyrin ruffling are reported. Both heme proteins obey a similar excellent linear δ ( C) versus ν (C–O) relationship which is primarily due to modulation π-back-bonding from d π CO * orbital by pocket interactions. The lack correlation between O) suggests that two probes do not reflect type electronic structural perturbation. influenced local field interactions does correlate any single property Fe–C–O unit; however, atropisomerism deformation geometry appear play significant role. shieldings vary nearly 900 ppm among various hemes an was found Fe) absolute crystallographic average displacement meso carbon atoms, | C m |, relative core mean plane. iron-57 carbons skeleton TPP derivatives perturbation ruffling.