2016 Fiscal Year Final Research Report
Study on Dioxygen Reduction Mechanism by Multicopper Oxidases and Application of Function Modulated Mutants as Electrode Catalyst
| Project/Area Number |
26288076
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bio-related chemistry
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| Research Institution | Kanazawa University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
片岡 邦重 金沢大学, 物質化学系, 教授 (40252712)
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| Co-Investigator(Renkei-kenkyūsha) |
KOMORI Hirofumi 香川大学, 教育学部, 准教授 (30382261)
TSUJIMURA Seiya 筑波大学, 数理物質科学研究科, 准教授 (30362429)
IDA Tomonori 金沢大学, 物質化学系, 准教授 (30345607)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Keywords | マルチ銅オキシダーゼ / 酸素４電子還元 / 機能改変 / 電極触媒 / CueO / ビリルビンオキシダーゼ |
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| Outline of Final Research Achievements |
Studies on the three-domain multicopper oxidases such as CueO and bilirubin oxidase by the mutations at the type I copper ligand and/or the acidic amino acid located in the proton transport pathway revealed that the four-electron reduction of dioxygen proceeds according to a common reaction pathway. Amino acids located in the outer-sphere of the trinuclear copper center were found not to play a role as the fourth electron donor. From the finding that an acetate ion from buffer solution was bound to type II copper, it was found that this exogenous anion reaches deep inside protein molecule and enhances enzymatic activities. Further, we performed crystallization of CueO in heavy water for neutral diffraction to reveal the reaction mechanism. We also succeeded in enhancing enzymatic activities by performing mutations at the amino acids located in the outer-coordination spheres of type I copper and obtained excellent electrochemical responses suitable as cathodic enzyme for biofuel cell.
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| Free Research Field |
生化学
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