Protein dynamics. Comparative investigation on heme-proteins with different physiological roles.
We report the low temperature carbon monoxide recombination kinetics after photolysis and the temperature dependence of the visible absorption spectra of the isolated alpha SH-CO and beta SH-CO subunits from human hemoglobin A in ethylene glycol/water and in glycerol/water mixtures. Kinetic measurem...
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1991
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ftcdlib:oai:escholarship.org/ark:/13030/qt7c71x3bn 2023-05-15T18:26:52+02:00 Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. Di Iorio, EE Hiltpold, UR Filipovic, D Winterhalter, KH Gratton, E Vitrano, E Cupane, A Leone, M Cordone, L 742 - 754 1991-03-01 application/pdf https://escholarship.org/uc/item/7c71x3bn unknown eScholarship, University of California qt7c71x3bn https://escholarship.org/uc/item/7c71x3bn CC-BY CC-BY Biophysical journal, vol 59, iss 3 Animals Humans Carbon Monoxide Hemoglobin A Myoglobin Hemeproteins Spectrophotometry Biophysics Kinetics Photolysis Thermodynamics Biophysical Phenomena In Vitro Techniques Physical Sciences Chemical Sciences Biological Sciences article 1991 ftcdlib 2021-02-18T15:14:24Z We report the low temperature carbon monoxide recombination kinetics after photolysis and the temperature dependence of the visible absorption spectra of the isolated alpha SH-CO and beta SH-CO subunits from human hemoglobin A in ethylene glycol/water and in glycerol/water mixtures. Kinetic measurements on sperm whale (Physeter catodon) myoglobin and previously published optical spectroscopy data on the latter protein and on human hemoglobin A, in both solvents, (Cordone, L., A. Cupane, M. Leone, E. Vitrano, and D. Bulone. 1988. J. Mol. Biol. 199:312-218) are taken as reference. Low temperature flash photolysis data are analyzed within the multiple substates model proposed by Frauenfelder and co-workers (Austin, R. H., K. W. Beeson, L. Eisenstein, H. Frauenfelder, and I. C. Gunsalus. 1975. Biochemistry. 14:5355-5373). Within this model a distribution of activation enthalpies for ligand binding accounts for the structural heterogeneity of the protein, while the preexponential factor, containing also the entropic contribution to the free energy of the process, is considered to be constant for all conformational substates. Optical spectra are deconvoluted in gaussian components and the temperature dependence of the moments of the resulting bands is analyzed, within the harmonic Frank-Condon approximation, to obtain information on the stereodynamic properties of the heme pocket. The kinetic and spectral parameters thus obtained are found to be protein dependent also with respect to their sensitivity to changes in the composition of the external medium. A close correlation between the kinetic and spectral features is observed for the proteins examined under all experimental conditions studied. The results reported are discussed in terms of differences in the heme pocket structure and in the conformational heterogeneity among the various proteins, as related to their different capability to accommodate constraints imposed by the external medium. Article in Journal/Newspaper Sperm whale University of California: eScholarship Austin Catodon ENVELOPE(-59.966,-59.966,-63.500,-63.500) |
institution |
Open Polar |
collection |
University of California: eScholarship |
op_collection_id |
ftcdlib |
language |
unknown |
topic |
Animals Humans Carbon Monoxide Hemoglobin A Myoglobin Hemeproteins Spectrophotometry Biophysics Kinetics Photolysis Thermodynamics Biophysical Phenomena In Vitro Techniques Physical Sciences Chemical Sciences Biological Sciences |
spellingShingle |
Animals Humans Carbon Monoxide Hemoglobin A Myoglobin Hemeproteins Spectrophotometry Biophysics Kinetics Photolysis Thermodynamics Biophysical Phenomena In Vitro Techniques Physical Sciences Chemical Sciences Biological Sciences Di Iorio, EE Hiltpold, UR Filipovic, D Winterhalter, KH Gratton, E Vitrano, E Cupane, A Leone, M Cordone, L Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
topic_facet |
Animals Humans Carbon Monoxide Hemoglobin A Myoglobin Hemeproteins Spectrophotometry Biophysics Kinetics Photolysis Thermodynamics Biophysical Phenomena In Vitro Techniques Physical Sciences Chemical Sciences Biological Sciences |
description |
We report the low temperature carbon monoxide recombination kinetics after photolysis and the temperature dependence of the visible absorption spectra of the isolated alpha SH-CO and beta SH-CO subunits from human hemoglobin A in ethylene glycol/water and in glycerol/water mixtures. Kinetic measurements on sperm whale (Physeter catodon) myoglobin and previously published optical spectroscopy data on the latter protein and on human hemoglobin A, in both solvents, (Cordone, L., A. Cupane, M. Leone, E. Vitrano, and D. Bulone. 1988. J. Mol. Biol. 199:312-218) are taken as reference. Low temperature flash photolysis data are analyzed within the multiple substates model proposed by Frauenfelder and co-workers (Austin, R. H., K. W. Beeson, L. Eisenstein, H. Frauenfelder, and I. C. Gunsalus. 1975. Biochemistry. 14:5355-5373). Within this model a distribution of activation enthalpies for ligand binding accounts for the structural heterogeneity of the protein, while the preexponential factor, containing also the entropic contribution to the free energy of the process, is considered to be constant for all conformational substates. Optical spectra are deconvoluted in gaussian components and the temperature dependence of the moments of the resulting bands is analyzed, within the harmonic Frank-Condon approximation, to obtain information on the stereodynamic properties of the heme pocket. The kinetic and spectral parameters thus obtained are found to be protein dependent also with respect to their sensitivity to changes in the composition of the external medium. A close correlation between the kinetic and spectral features is observed for the proteins examined under all experimental conditions studied. The results reported are discussed in terms of differences in the heme pocket structure and in the conformational heterogeneity among the various proteins, as related to their different capability to accommodate constraints imposed by the external medium. |
format |
Article in Journal/Newspaper |
author |
Di Iorio, EE Hiltpold, UR Filipovic, D Winterhalter, KH Gratton, E Vitrano, E Cupane, A Leone, M Cordone, L |
author_facet |
Di Iorio, EE Hiltpold, UR Filipovic, D Winterhalter, KH Gratton, E Vitrano, E Cupane, A Leone, M Cordone, L |
author_sort |
Di Iorio, EE |
title |
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
title_short |
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
title_full |
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
title_fullStr |
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
title_full_unstemmed |
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. |
title_sort |
protein dynamics. comparative investigation on heme-proteins with different physiological roles. |
publisher |
eScholarship, University of California |
publishDate |
1991 |
url |
https://escholarship.org/uc/item/7c71x3bn |
op_coverage |
742 - 754 |
long_lat |
ENVELOPE(-59.966,-59.966,-63.500,-63.500) |
geographic |
Austin Catodon |
geographic_facet |
Austin Catodon |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biophysical journal, vol 59, iss 3 |
op_relation |
qt7c71x3bn https://escholarship.org/uc/item/7c71x3bn |
op_rights |
CC-BY |
op_rightsnorm |
CC-BY |
_version_ |
1766208835722149888 |