Tertiary-structure relaxation in hemoglobin: a transient Raman study
- 1 September 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 106 (19) , 5677-5687
- https://doi.org/10.1021/ja00331a044
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Kinetics of hemoglobin and transition state theory.Proceedings of the National Academy of Sciences, 1978
- Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin.Proceedings of the National Academy of Sciences, 1978
- Nitrosylmetalloporphyrins. 4. Molecular stereochemistry of two crystalline forms of nitrosyl-.alpha.,.beta.,.gamma.,.delta.-tetraphenylporphinato(4-methylpiperidine)iron(II). A structural correlation with .nu.(NO)Journal of the American Chemical Society, 1977
- Energy-structure correlation in metalloporphyrins and the control of oxygen binding by hemoglobin.Proceedings of the National Academy of Sciences, 1977
- Molecular description of dioxygen bonding in hemoglobin.Proceedings of the National Academy of Sciences, 1977
- Mechanism of tertiary structural change in hemoglobin.Proceedings of the National Academy of Sciences, 1977
- Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4.Journal of Biological Chemistry, 1976
- Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: interpretation of electron spin resonance spectraBiochemistry, 1976
- Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogsJournal of the American Chemical Society, 1976
- The photochemical formation of a quickly reacting form of haemoglobinBiochemical Journal, 1959