Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR
The proton nuclear magnetic resonance spectra of soybean ferric leghemoglobin a in the low-spin cyanide and nicotinate complexes have been assigned by specific deuteration of heme methyl groups. The assignments differ from those obtained solely from nuclear Overhauser enhancement measurements and are indicative of a proximal histidyl imidazole-hemin interaction which is very similar to that found in sperm whale myoglobin. The absence of a hyperfine shifted exchangeable NH peak for the distal histidine in leghemoglobin suggests either a very different orientation for this distal ligand or a significantly faster exchange rate with bulk solvent than found in myoglobin. © 1981.
Publication Source (Journal or Book title)
Biochemical and Biophysical Research Communications
La Mar, G., Kong, S., Smith, K., & Langry, K. (1981). Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR. Biochemical and Biophysical Research Communications, 102 (1), 142-148. https://doi.org/10.1016/0006-291X(81)91500-X