Time-resolved ultraviolet resonance Raman study of the photolysis of carbomonoxyhemoglobin. Relaxation of the globin structure
- 1 January 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 112 (1) , 23-27
- https://doi.org/10.1021/ja00157a006
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- 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
- Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scatteringJournal of Molecular Biology, 1980
- Spin equilibrium and quaternary structure change in hemoglobin A. Experiments on a quantitative probe of the stereochemical mechanism of hemoglobin cooperativityBiochemistry, 1979
- Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobinProceedings of the National Academy of Sciences, 1979
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- The Raman spectra of Bence‐Jones proteins. Disulfide stretching frequencies and dependence of Raman intensity of tryptophan residues on their environmentsBiopolymers, 1979
- Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation.Proceedings of the National Academy of Sciences, 1978
- Time-Resolved Resonance Raman Spectroscopy of Hemoglobin Derivatives: Heme Structure Changes in 7 NanosecondsScience, 1978
- Structure of human fluoromethaemoglobin with inositol hexaphosphateJournal of Molecular Biology, 1977
- Time-Resolved Spectroscopy of Hemoglobin and Its Complexes with Subpicosecond Optical PulsessScience, 1976