The 400 MHz 1H-NMR spectra of the O2 and CO complexes of ferrous soybean leghamoglobin α are reported. Spain decoupling and proton-proton nuclear Overhauser effect experiments have allowed specific assignment of the resonances of all of the heme substituent groups except the propionic acid side-chains. The resonances of the side chains of the important distal amino acids, Ph-44, His-61 and Leu-65, and the C-4 proton of the proximal histidine (His-92) have also been assigned. The NMR spectra indicate substantial conformational differences near the heme in oxy- and carbonmonoxyleghemoglobin. There appear to be no significant differences in the iron-proximal histidine distance.
|Number of pages||10|
|Journal||Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular|
|Publication status||Published - 18 May 1983|
- Amino Acid
- Heme group