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Accession number;02A0421399
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| Title;Towards Studies of Biomolecular Science using Fortes of Vibrational Spectroscopy. |
| Author;
KITAGAWA TEIZO
(Okazakikokuritsukyodokenkyukiko Togobaiosaiensuse)
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Journal Title;Nippon Kagakkai Koen Yokoshu
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Journal Code:S0493A
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ISSN:0285-7626
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VOL.81st;NO.1;PAGE.A.2(2002)
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| Figure&Table&Reference;REF.4 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Our group has made efforts towards advanced studies of biomolecular science through sharp application of vibrational spectroscopy. A few oxygen activating heme enzymes besides myoglobins and hemoglobins have been used as materials to investigate some basic phenomena including biological activation of oxygen, bioenergetics, structural mechanism of allosteric effects, and fast dynamics of proteins. Techniques used are mainly time-resolved resonance Raman spectroscopy in a time range from picoseconds to milliseconds as well as static visible- and UV-excited Raman scattering and infrared absorption. Our finding of the Fe-His stretching band of hemoglobin revived Perutz's strain model of oxygen affinity, and the band nowadays attracts notice from a view of signal transduction of heme sensor proteins. Observations of oxygen-isotope sensitive bands for all the reaction intermediates of bovine cytochrome c oxidase renewed its enzymatic cycle, which is now cited in a textbook. Picosecond anti-Stokes Raman revealed cooling dynamics of myoglobin after CO photolysis. (author abst.) |
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