19 research outputs found
NMR studies of hemoproteins: pH dependence of ferric horseradish peroxidase and horse heart myoglobin
Get PDFCharacterization of neutrophil b-type cytochrome in situ by electron paramagnetic resonance spectroscopy
Get PDFAbstractElectron paramagnetic resonance spectroscopy at 4.2 K was successfully used to characterize neutrophil b-type cytochrome in situ. The spectra or resting neutrophils taken under aerobic conditions gave a set of characteristic signals in a high magnetic field (g=2.85, 2.21 and 1.67) beside signals for myeloperoxidase and others. From the g values, shapes and the results of other experiments, these signals were attributed to those of cytochrome b558. The results indicate that cytochrome b558 in resting neutrophils is a hexa-coordinated ferric hemoprotein in a low-spin state. The obtained g??? and g??? values for the hemichrome were consistent with that of bis(imiduzole)-coordinated hemoprotein
Roles of Ile209 and Ile210 on the Heme Pocket Structure and Regulation of Histidine Kinase Activity of Oxygen Sensor FixL from Rhizobium meliloti
No full textNMR studies of hemoproteins: pH dependence of ferric horseradish peroxidase and horse heart myoglobin
No full textAnalysis of thermal equilibrium between high-spin and low-spin states in ferrimyoglobin complexes
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Correlation between the quantum yields of photodissociation and CO stretching frequencies of carbon monoxide hemoproteins
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