The apparent quantum yield of T-state human hemoglobin. Contribution of protein and heme to rates of oxygen reactions.
Open Access
- 1 January 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (1) , 365-371
- https://doi.org/10.1016/s0021-9258(17)43668-4
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobinJournal of Molecular Biology, 1983
- Femtosecond photodissociation and picosecond recombination of O2 in myoglobin: A plausible explanation for the low quantum yield in MbO2Biochemical and Biophysical Research Communications, 1982
- Nanosecond laser photolysis of aqueous carbon monoxy- and oxyhaemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- A gas—Liquid equilibration apparatus for quantitative determination of oxygen binding by hemoglobinAnalytical Biochemistry, 1976
- Time-Resolved Spectroscopy of Hemoglobin and Its Complexes with Subpicosecond Optical PulsessScience, 1976
- Dynamics of ligand binding to myoglobinBiochemistry, 1975
- Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromoleculesBiochemistry, 1973
- Studies on the Quantum Yields of the Photodissociation of Carbon Monoxide from Hemoglobin and Myoglobin*Biochemistry, 1967
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- The Freshwater Eel Anguilla obscura Gunther, 1871, in Southern AfricaNature, 1957