2009 Fiscal Year Final Research Report
Kinetic and X-ray crystallographic analysis of quantum mechanical hydrogen tunneling in enzyme-catalyzed reaction
| Project/Area Number |
19770118
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | Osaka Medical College |
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Principal Investigator |
MURAKAWA Takeshi Osaka Medical College, 医学部, 助教 (90445990)
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| Project Period (FY) |
2007 – 2009
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| Keywords | プロトントンネリング / ビルトインキノン補酵素 / 同位体効果 |
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| Research Abstract |
It is becoming widely accepted that the hydrogen tunneling is a general feature of the enzyme-catalyzed reaction at room temperature, especially in the reaction requiring high activation energy such as C-H bond cleavage. We analyzed stereospecific abstraction of substrate ・^-proton catalyzed by copper amine oxidases from Arthrobacter globiformis (AGAO) by transition-state kinetics and X-ray crystallographic analysis. These results provide new finding for enzyme-enhanced hydrogen tunneling.
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