Studies on Chemical Functions of Novel Redox Coenzymes
Grant-in-Aid for Scientific Research (B)
|Allocation Type||Single-year Grants |
|Research Institution||Osaka University |
ITOH Shinobu Osaka University, Faculty of Engineering, Department of Applied Chemistry, Associate Professor, 工学部, 助教授 (30184659)
SUENOBU Tomoyoshi Osaka University, Faculty of Engineering, Department of Applied Chemistry, Resea, 工学部, 助手 (90271030)
FUKUZUMI Shunichi Osaka University, Faculty of Engineering, Department of Applied Chemistry, Profe, 工学部, 教授 (40144430)
|Project Period (FY)
1996 – 1997
Completed (Fiscal Year 1997)
|Budget Amount *help
¥7,300,000 (Direct Cost: ¥7,300,000)
Fiscal Year 1997: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1996: ¥5,700,000 (Direct Cost: ¥5,700,000)
|Keywords||Coenzyme / Pyrroloquinolinequione / Tryptophan Tryptophylquinone / Alcohol Dehydrogenase / Amino Dehydrogenase / Galactose Oxidase / Redox Reaction / Model Study / 補酵素モデル / 反応機構 / キノプロテイン / オルトキノン / PQQ / TTQ / モデル銅錯体 / 銅錯体|
In this research project, the physicochemical properties and chemical functions of novel redox coenzymes such as PQQ (pyrroloquinolinequinone) of bacterial alcohol and glucose dehydrogenases, TTQ (tryptophan tryptophylquinone) of bacterial amine dehydrogenases, and Tyr-Cys (a dimer of tyrosine and cysteine) of galactose oxidase have been explored. Followings are the summary of the results.
・Model studies on quinoprotein methanol dehydrogenase has been carried out to find that the oxidation of methanol by calcium complex of coenzyme PQQ proceeds via addition-elimination mechanism. The catalytic role of calcium ion on the methanol oxidation has been also explored.
・Catalysis by calcium ion on the reoxidation of reduced PQQ by molecular oxygen has been investigated.
・Electrochemical behavior of coenzyme PQQ in aprotic organic media has been explored.
・Photochemical oxidation of benzyl alcohols by the triplet excited state of coenzyme PQQ has been explored.
・Photochemical redox react
ions of coenzyme PQQ and related o-quinones have been investigated in detail.
・Novel addition-cyclization reaction of nitroalkane anions with o-quinone derivatives has been found to proceed via electron transfer in the charge-transfer complexes.
・Model studies of TTQ-containing amine dehydrogenases has been performed to clarify the amine oxidation mechanism by TTQ coenzyme.
・Electrostatic environment of the TTQ cofactor in methylamine dehydrogenase has been investigated by using TTQ model compounds.
・Synthesis, physicochemical properties, and amine-oxidation reaction ofindolequinone derivatives as model compounds of novel organic cofactor TTQ of amine dehydrogenases have been investigated.
・Active site models for galactose oxidase have been developed in order to shed light on the electronic effect of the thioether group in the novel organic cofactor.
・Active site models for galactose oxidase have been developed in order to study the physicochemical properties and reactivities of copper (II) complex of the phenoxyl radical species of the novel organic cofactor. Less
Report (3 results)
Research Products (34 results)