Carbon-13 NMR studies of C2H5N13C binding to various hemoproteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference10 articles.
1. Natural abundance 13 C spectra of proteins: Carboxy-myoglobin and hemoglobin
2. Nuclear magnetic resonance studies of carbon-13 monoxide binding to various hemoglobins
3. Carbon-13 NMR studies of 13Co binding to human hemoglobin
4. Carbon-13 nuclear magnetic resonance and infrared spectroscopic studies of carbon-13 monoxide binding to rabbit hemoglobin
5. NMR studies of 13 CO-hemoglobin. α and β chain identification
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1. 13C and 15N NMR Studies of Iron-Bound Cyanides of Heme Proteins and Related Model Complexes: Sensitive Probe for Detecting Hydrogen-bonding Interactions at the Proximal and Distal Sides;Inorganic Chemistry;2006-07-25
2. Solid-State NMR, Crystallographic and Density Functional Theory Investigation of Fe−CO and Fe−CO Analogue Metalloporphyrins and Metalloproteins;Journal of the American Chemical Society;1999-04-01
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. Binding of ethyl isocyanide to cytochrome c′ from Chromatium vinosum;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1983-03
5. 13C nuclear magnetic resonance studies of the binding of alkyl isocyanides to soybean leghemoglobin; comparison with animal myoglobins;Biochimie;1980-12
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