2009 Fiscal Year Final Research Report
Studies on the structure and function of hemeproteins that use advantage of introduction of fluoroalkyl groups
| Project/Area Number |
19550172
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Nagaoka National College of Technology |
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Principal Investigator |
SUZUKI Akihiro Nagaoka National College of Technology, 物質工学科, 教授 (60179190)
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| Project Period (FY) |
2007 – 2009
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| Keywords | 生物有機化学 |
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| Research Abstract |
Functional regulation of hemeprotein is thought to be achieved through electronic structure of heme, and heme environment furnished by nearby amino acid residues. In this study, I have performed substitution of electron-withdrawing fluoro (F) and perfluoromethyl (CF_3) group(s) as pyrrole, porphyrin and heme side chain(s) to obtain large alteration of the heme electronic structure in order to elucidate the relationship between the structure and function. I have measured the ^<19>F-NMR, and the equilibrium constant (pKa) of the "acid-alkaline transition" in metmyoglobin in order to quantitatively assess the effects of the F and CF_3 substitutions for the electron density of heme Fe atom of the hemeprotein. I have confirmed that the introduction of F or CF_3 group(s) to the heme side chain(s) leads to a decrease in the electron density of the heme Fe atom, which in turn decreases the O_2 affinity of hemeprotein.
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[Journal Article] Effect of Heme Modification on Oxygen Affinity of Myoglobin and Equilibrium of the Acid-Alkaline Transition in Metmyoglobin2010
Author(s)
T. Shibata, S. Nagao, M. Fukaya, H. Tai, S. Nagatomo, K. Morihashi, T. Matsuo, S. Hirota, A. Suzuki, K. Imai, Y. Yamamoto
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Journal Title
Journal of the American Chemical Society 132
Pages: 6091-6098
Peer Reviewed
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