Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation.
- 1 November 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 75 (11), 5255-5259
- https://doi.org/10.1073/pnas.75.11.5255
Abstract
The photolysis of [human] HbO2 and HbCO was investigated with ps laser techniques. Transient absorption spectra were measured in the Soret and visible regions after excitation with 353- or 530-nm pulses. The photoproducts appeared within 8 ps and exhibited considerably broadened deoxyhemoglobin-like spectra, which persisted to 680 ps. The altered spectra were attributed to the production of deoxyheme conformational and spin states that might result from intense excitation.This publication has 22 references indexed in Scilit:
- Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin.Proceedings of the National Academy of Sciences, 1978
- Binding of carbon monoxide to isolated hemoglobin chainsBiochemistry, 1978
- On the photosensitivity of liganded hemoproteins and their metal-substituted analogues.Proceedings of the National Academy of Sciences, 1978
- Properties of the T state of human oxyhemoglobin studies by laser photolysis.Journal of Biological Chemistry, 1977
- Photodissociation of ligands from heme and heme proteins. Effect of temperature and organic phosphate.Journal of Biological Chemistry, 1977
- Mechanism of tertiary structural change in hemoglobin.Proceedings of the National Academy of Sciences, 1977
- Rate of quaternary structure change in hemoglobin measured by modulated excitation.Proceedings of the National Academy of Sciences of the United States of America, 1976
- Dynamics of ligand binding to myoglobinBiochemistry, 1975
- Studies on the Quantum Yields of the Photodissociation of Carbon Monoxide from Hemoglobin and Myoglobin*Biochemistry, 1967
- The photochemical formation of a quickly reacting form of haemoglobinBiochemical Journal, 1959