Stark-effect spectroscopy of the heme charge-transfer bands of deoxymyoglobin

Article Abstract:

The Stark spectra of the Soret, Q and charge-transfer bands of deoxymyoglobin has been observed to have distinct features. The broad negative base line offset seen below 16,000/cm may be due to the Stark effect on band II. Band III has charge-transfer characteristics but the charge displacement is smaller than in band I or the Soret or Q bands. It has also been noted that the symmetry breaking of iron-protoporphyrin IX in myoglobin results in a higher difference dipole moment in the Soret band.

Analysis, Spectra, Porphyrins, Heme

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Resonance Raman studies of heme axial ligation in H93G myoglobin

Article Abstract:

The resonant Raman active mode identified in numerous studies as the heme iron-histidine stretch in the Raman spectrum of 15 exogenous ligands to the heme iron in the myoglobin proximal cavity mutant H93g is investigated. It is seen that Raman bands attributed to in-plane modes of the heme are unaffected by the change in heme-iron ligation.

Oxidases, Iron compounds, Chemical properties

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Dependence of NO recombination dynamics in horse myoglobin on solution glycerol content

Article Abstract:

Research is presented describing how NO recombination in horse heart myoglobin at room temperature is affected by the glycerol content of the buffer solution.

Research, Biochemistry, Physiological aspects, Horses, Glycerol, Hemoproteins

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