Photothermal Studies of Carboxymyoglobin
Small ligand diffusion in heme proteins is not fully understood. To help better understand CO diffusion, three systems were investigated: L29H/F43H site-directed sperm whale myoglobin, horse heart myoglobin in a heavy water buffer, and calix[4]resorcinarene. Binding of copper to calix[4]resorcinaren...
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Digital Commons @ University of South Florida
2010
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ftusouthflorida:oai:digitalcommons.usf.edu:etd-2774 2023-07-30T04:07:06+02:00 Photothermal Studies of Carboxymyoglobin Small, Meagan 2010-07-15T07:00:00Z application/pdf https://digitalcommons.usf.edu/etd/1775 https://digitalcommons.usf.edu/context/etd/article/2774/viewcontent/.pdf unknown Digital Commons @ University of South Florida https://digitalcommons.usf.edu/etd/1775 https://digitalcommons.usf.edu/context/etd/article/2774/viewcontent/.pdf default USF Tampa Graduate Theses and Dissertations myoglobin thermodynamics heme proteins calixarenes photoacoustic calorimetry American Studies Arts and Humanities thesis 2010 ftusouthflorida 2023-07-13T21:35:03Z Small ligand diffusion in heme proteins is not fully understood. To help better understand CO diffusion, three systems were investigated: L29H/F43H site-directed sperm whale myoglobin, horse heart myoglobin in a heavy water buffer, and calix[4]resorcinarene. Binding of copper to calix[4]resorcinarene was photophysically characterized to unravel transient binding of small molecules in heme-copper proteins. Copper binding was found to have a low dissociation constant of approximately 8.6 micrometers. Reaction profiles using photoacoustic calorimetry were constructed for the myoglobin systems. In deuterium oxide, ligand escape is not rate limited by water entry. Large enthalpy differences arise from the thermodynamic properties of deuterium oxide and the extensive hydrogen bonding network in myoglobin. In the mutant, CO rebinds primarily to the heme and is exothermic with a large volume contraction because of altered electrostatics within the binding pocket and higher water occupancy. Thesis Sperm whale University of South Florida St. Petersburg: Digital USFSP |
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Open Polar |
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University of South Florida St. Petersburg: Digital USFSP |
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ftusouthflorida |
language |
unknown |
topic |
myoglobin thermodynamics heme proteins calixarenes photoacoustic calorimetry American Studies Arts and Humanities |
spellingShingle |
myoglobin thermodynamics heme proteins calixarenes photoacoustic calorimetry American Studies Arts and Humanities Small, Meagan Photothermal Studies of Carboxymyoglobin |
topic_facet |
myoglobin thermodynamics heme proteins calixarenes photoacoustic calorimetry American Studies Arts and Humanities |
description |
Small ligand diffusion in heme proteins is not fully understood. To help better understand CO diffusion, three systems were investigated: L29H/F43H site-directed sperm whale myoglobin, horse heart myoglobin in a heavy water buffer, and calix[4]resorcinarene. Binding of copper to calix[4]resorcinarene was photophysically characterized to unravel transient binding of small molecules in heme-copper proteins. Copper binding was found to have a low dissociation constant of approximately 8.6 micrometers. Reaction profiles using photoacoustic calorimetry were constructed for the myoglobin systems. In deuterium oxide, ligand escape is not rate limited by water entry. Large enthalpy differences arise from the thermodynamic properties of deuterium oxide and the extensive hydrogen bonding network in myoglobin. In the mutant, CO rebinds primarily to the heme and is exothermic with a large volume contraction because of altered electrostatics within the binding pocket and higher water occupancy. |
format |
Thesis |
author |
Small, Meagan |
author_facet |
Small, Meagan |
author_sort |
Small, Meagan |
title |
Photothermal Studies of Carboxymyoglobin |
title_short |
Photothermal Studies of Carboxymyoglobin |
title_full |
Photothermal Studies of Carboxymyoglobin |
title_fullStr |
Photothermal Studies of Carboxymyoglobin |
title_full_unstemmed |
Photothermal Studies of Carboxymyoglobin |
title_sort |
photothermal studies of carboxymyoglobin |
publisher |
Digital Commons @ University of South Florida |
publishDate |
2010 |
url |
https://digitalcommons.usf.edu/etd/1775 https://digitalcommons.usf.edu/context/etd/article/2774/viewcontent/.pdf |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
USF Tampa Graduate Theses and Dissertations |
op_relation |
https://digitalcommons.usf.edu/etd/1775 https://digitalcommons.usf.edu/context/etd/article/2774/viewcontent/.pdf |
op_rights |
default |
_version_ |
1772820210868289536 |