Activating the phosphate nucleophile at the catalytic site of purine nucleoside phosphorylase: A vibrational spectroscopic study

被引：39

作者：

Deng, H ^{[1
]}

Lewandowicz, A ^{[1
]}

Schramm, VL ^{[1
]}

Callender, R ^{[1
]}

机构：

[1] Yeshiva Univ Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 31期

关键词：

D O I：

10.1021/ja049296p

中图分类号：

O6 [化学];

学科分类号：

0703 [化学];

摘要：

Difference Raman and FTIR studies complemented by vibrational analysis based on ab initio calculations show that the dianionic phosphate in the PNP·ImmH·PO4 complex is forced into a unique bonding arrangement in which one of the P-O bonds is greatly polarized by enzyme active site interactions, such that it resembles a PO bond that is about one-quarter of the way toward forming a bridging P-O-C single P-O bond. Copyright © 2004 American Chemical Society.

引用

页码：9516 / 9517

页数：2

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