Artificial Trinuclear Metallopeptidase Synthesized by Cross-Linkage of a Molecular Bowl with a Polystyrene Derivative
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- 作者：Sung-Ju Moon ; Joong Won Jeon ; Heesuk Kim ; Myunghyun Paik Suh ; and Junghun Suh
- 刊名：Journal of the American Chemical Society
- 出版年：2000
- 出版时间：August 16, 2000
- 年：2000
- 卷：122
- 期：32
- 页码：7742 - 7749
- 全文大小：295K
- 年卷期：v.122,no.32(August 16, 2000)
- ISSN：1520-5126
文摘
A novel methodology is reported for construction of active sites of artificial multinuclearmetalloenzymes: transfer of metal-chelating sites confined in a prebuilt cage to a polymeric backbone. Artificialactive sites comprising two or three moieties of Cu(II) complex of tris(2-aminoethyl)amine (tren) were preparedby transfer of Cu(II)tren units confined in a molecular bowl (MB) to poly(chloromethylstyrene-co-divinylbenzene) (PCD). By treatment of unreacted chloro groups of the resulting PCD with methoxide anddestruction of the MB moieties attached to PCD with acid followed by addition of Cu(II) ion to the exposedtren moieties, catalytic polymers with peptidase activity were obtained. The average number (
) of proximalCu(II)tren moieties in the active site of the artificial multinuclear metallopeptidase was determined by quantifyingthe Cu(II) content. Several species of the artificial metallopeptidases with different contents were preparedand examined for catalytic activity in hydrolysis of various cinnamoyl amide derivatives. The PCD-basedcatalytic polymers did not hydrolyze a neutral amide but effectively hydrolyzed carboxyl-containing amides(N-cinnamoyl glycine, N-cinnamoyl -alanine, and N-cinnamoyl 
-amino butyrate). Analysis of the kineticdata revealed that the active sites comprising three Cu(II)tren units were mainly responsible for the catalyticactivity. When analyzed in terms of kcat, the catalytic activity of the PCD-based artificial peptidase wascomparable to or better than the catalytic antibody with the highest peptidase activity reported to date. Amechanism is suggested for the effective cooperation among the three metal centers of the active site in hydrolysisof the carboxyl-containing amides.
) of proximalCu(II)tren moieties in the active site of the artificial multinuclear metallopeptidase was determined by quantifyingthe Cu(II) content. Several species of the artificial metallopeptidases with different contents were preparedand examined for catalytic activity in hydrolysis of various cinnamoyl amide derivatives. The PCD-basedcatalytic polymers did not hydrolyze a neutral amide but effectively hydrolyzed carboxyl-containing amides(N-cinnamoyl glycine, N-cinnamoyl -alanine, and N-cinnamoyl -amino butyrate). Analysis of the kineticdata revealed that the active sites comprising three Cu(II)tren units were mainly responsible for the catalyticactivity. When analyzed in terms of kcat, the catalytic activity of the PCD-based artificial peptidase wascomparable to or better than the catalytic antibody with the highest peptidase activity reported to date. Amechanism is suggested for the effective cooperation among the three metal centers of the active site in hydrolysisof the carboxyl-containing amides.