NMR titration curves of histidine ring protons. 11. Near-heme histidine residues of deoxy- and oxymyoglobins
- 17 April 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (8), 1599-1602
- https://doi.org/10.1021/bi00575a034
Abstract
Proton NMR titration curves of the histidine C.epsilon.-H resonances of the deoxy and oxy forms of human, horse and sperm whale myoglobins (Mb) were determined and compared with the results for the met and azide forms. One extra titrating resonance (H-8) was observed for each deoxy-Mb compared with the corresponding met-Mb, and an extra resonance (H-9) was observed for the oxy-Mb form. These resonances correspond to the 2 additional resonances previously described for azide-Mb. These resonances should be assigned to the near-heme histidine residues.This publication has 7 references indexed in Scilit:
- Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species. Specific assignment of individual resonancesBiochemistry, 1978
- Proton nuclear magnetic resonance study of histidine ionizations in myoglobins of various species. Comparison of observed and computed pK valuesBiochemistry, 1978
- A proton magnetic resonance study of the distal histidine of soybean Leghemoglobin. Effects of nicotinate and other heme ligands.Journal of Biological Chemistry, 1978
- Titration behavior and tautomeric states of individual histidine residues of myoglobins. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy.Journal of Biological Chemistry, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- The mode of attachment of the azide ion to sperm whale metmyoglobinJournal of Molecular Biology, 1964