Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes
- 1 September 1985
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 131 (2) , 607-613
- https://doi.org/10.1016/0006-291x(85)91280-x
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and ZurichJournal of the American Chemical Society, 1985
- Carbon-13 nuclear magnetic resonance comparison of the crystalline and solution states of carbonyl hemoglobin AJournal of the American Chemical Society, 1980
- Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensitiesBiochemistry, 1978
- Magnetic resonance studies of the binding of 13C-labeled carbon monoxide to myoglobins and hemoglobins containing modified hemesBiochemistry, 1977
- Carbon-13 magnetic resonance studies of the binding of carbon monoxide to various hemoglobinsBiochemistry, 1974
- Carbon-13 NMR studies of 13Co binding to human hemoglobinBiochemical and Biophysical Research Communications, 1973
- NMR studies of 13CO‐hemoglobin. α and β chain identificationFEBS Letters, 1973
- Carbon-13 nmr spectroscopy of red blood cell suspensionsBiochemical and Biophysical Research Communications, 1972
- Nuclear magnetic resonance studies of carbon-13 monoxide binding to various hemoglobinsJournal of the American Chemical Society, 1972
- Natural abundance 13C spectra of proteins: Carboxy‐myoglobin and hemoglobinFEBS Letters, 1971