2000 Fiscal Year Final Research Report Summary
Construction of Sophisticated Flavin Catalytic Systems
| Project/Area Number |
10440183
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Organic chemistry
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| Research Institution | Gunma University |
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Principal Investigator |
YANO Yumihiko Gunma University, Faculty of Engineering Professor, 工学部, 教授 (30008510)
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| Co-Investigator(Kenkyū-buntansha) |
KONDO Shin-ichi Gunma University, Faculty of Engineering Assistant, 工学部, 助手 (20281503)
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| Project Period (FY) |
1998 – 2000
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| Keywords | Oxidation-active flavin / Artificial enzyme / Apoprotein model / Hydrogen bond / Functionalized flavin receptor / Guanidinium-melamine |
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| Research Abstract |
To establish the methodology for construction of artificial flavoenzymes, we have exploited functionalized oxidation-active flavin model and flavin receptors which bind the oxidation-active flavin via hydrogen bonds in organic solvents. We found for the first time that benzodipteridine bearing a-bipyridine moiety at the N (3)-position (bpy-BDP) oxidizes a-hydroxy acids in the presence of a divalent metal ion and a base in organic solvents (D-lactate Dehydrogenase model). The roles of the metal ion were clarified : the bound metal ion at the bipyridine moiety increases the oxidation activity of bpy-BDP by 10^2-10^3-fold by coordinating to the C(4)=O goup, attracts anionic substrate to form a complex, and activates the substrate.
It was found that melamine derivatives bearing guanidinium ion (s) strongly bind 6-azaflavin via five or seven hydrogen bonds in organic solvents such as chloroform. The hydrogen bondings shofted redox potentials of 6-azaflavin in a positive direction, stabilize the anionic semiquinone radical, and inctrease the oxidation-activity of 6-azaflavin. The functionalized melamine derivatives bearing a substrate-binding site or metal-binding site were found to exhibit more sophisticated systems, showing an apoprotein function.
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