2000 Fiscal Year Final Research Report Summary
FOUR-ELECTRON REDUCTION OF DIOXYGEN AT THE TRINUCLEAR COPPER CLUSTER IN MULTICOPPER OXIDASES
| Project/Area Number |
11640558
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Inorganic chemistry
|
|---|
| Research Institution | KANAZAWA UNIVERSITY |
|---|
Principal Investigator |
SAKURAI Takeshi KANAZAWA UNIVERSITY FACLTY OF SCIENCE PROFESSOR, 理学部, 教授 (90116038)
|
|---|
| Project Period (FY) |
1999 – 2000
|
| Keywords | multicopper oxidase / laccase / bilirubin oxidase / trinuclear Cu cluster / dioxygen reduction / hydroxyl radical / stopped-flow / ESR |
|---|
| Research Abstract |
The reactions of the reduced laccase and bilirubin oxidase with dioxygen were studied using mainly absorption and EPR spectra at a cryogenic temperature and also using stopped flow spectroscopy and SQUID magnetic measurement. The hydroxyl or oxyl radical bound to the trinuclear Cu site was detected as a reaction intermediate, three-electron reduced form of dioxygen, . Decays of this radical species were highly pH dependent on pH, indicating that the process was gated by the protonation to be water finally. A peroxide intermediate corresponding to the three electron reduced form of dioxygen could not be detected because diffusion of dioxygen to the trinuclear Cu site was rate-determining step and the electron transfer from type 1 Cu to the putative peroxide intermediate was very rapid. However, the peroxide intermediate could be detected by reaction dioxygen to the CuCl-acted type 2 Cu-depleted laccase under a strict anaerobic condition. Based on the successful detection and characterization of the two reaction intermediates the general reaction mechanism how dioxygen is four-electron reduced by multicopper oxidases was proposed.
|
Research Products
(10 results)
