New Function of Myoglobin Created by the Chemical Modification of Heme-Propionates.
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Accession number;02A0304384
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| Title;New Function of Myoglobin Created by the Chemical Modification of Heme-Propionates. |
| Author;
HAYASHI TAKASHI
(Kyushu Univ., Grad. Sch.)
ANDO TSUTOMU
(Kyushu Univ., Grad. Sch.)
MATSUDA TAKAAKI
(Kyushu Univ., Grad. Sch.)
HISAEDA YOSHIO
(Kyushu Univ., Grad. Sch.)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.56-57(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Myoglobin, one of the hemoproteins, is a well-known oxygen-storage protein which binds protoporphyrin IX iron complex via noncovalent interactions. To introduce a new function into the myoglobin, we have been carried out the modification of two heme-propionate side chains. For example, an artificially created charge cluster which is formed by the chemical modification of heme-propionates demonstrates a unique interface on the protein surface. Positively and negatively charged myoglobins can make stable complexes with some compounds and proteins having opposite charges. Particularly, photoinduced electron transfer from negatively charged zinc myoglobin to ferric cytochrome c occurs smoothly via the artificial interace on the myoglobin surface. Moreover, it is found that the chemical modirlcation of two heme-propionate enhances the peroxidase and peroxygenase activities due to the formation of hydrophobic pocket on the protein surface. Thioanisole and styrene are readily oxidized by ferryl species of the reconstituted myoglobin generated by hydrogen peroxide. In this presentation, we wish to demonstrate the new function of the reconstituted myoglobins with artificially created heme. (author abst.) |
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