Carbon-13 NMR studies of 13Co binding to human hemoglobin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference21 articles.
1. Nature of Haem–Haem Interaction
2. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
3. Nuclear magnetic resonance studies of carbon-13 monoxide binding to various hemoglobins
4. Carbon-13 nuclear magnetic resonance and infrared spectroscopic studies of carbon-13 monoxide binding to rabbit hemoglobin
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1. Substrate interactions in cytochrome P-450: correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies;FEBS Letters;1995-05-08
2. Carbon-13 and oxygen-17 NMR and IR spectroscopic study of a series of (carbonyl)(4-substituted pyridine)(meso-tetraphenylporphinato)iron(II) complexes. Correlations between NMR chemical shifts and IR stretching frequencies of the carbonyl ligand and Taft parameters of the pyridine substituent;Inorganic Chemistry;1987-08
3. Phosphines as a new structural probe of hemoglobin. 1H-NMR evidence for perturbations in the β heme pocket induced by a thiol reagent;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-08
4. Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes;Biochemical and Biophysical Research Communications;1985-09
5. [19] Carbon-13 nuclear magnetic resonance: New techniques;Enzyme Structure Part H;1979
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