Confirmation of the assignment of the iron-histidine stretching mode in myoglobin
- 1 October 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 106 (22) , 6593-6596
- https://doi.org/10.1021/ja00334a024
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Ligand, oxygen, and carbon monoxide affinities of iron(II) modified "capped" porphyrinsJournal of the American Chemical Society, 1982
- Protoheme conformations in low-spin ferrohemoproteins. Resonance raman spectroscopyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Low-frequency vibrations of ferroprotoporphyrin-substituted imidazole complexes. A resonance Raman studyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobinJournal of the American Chemical Society, 1980
- Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.Proceedings of the National Academy of Sciences, 1980
- Resonance raman study of the heme-linked ionization in reduced horseradish peroxidaseBiochemical and Biophysical Research Communications, 1980
- Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scatteringJournal of Molecular Biology, 1980
- Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modesBiochemistry, 1979
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.Proceedings of the National Academy of Sciences, 1979