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

Hua Deng; Andrzej Lewandowicz; Vern L. Schramm; Robert Callender

doi:10.1021/ja049296p

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

Hua Deng, Andrzej Lewandowicz, Vern L. Schramm, Robert Callender

Biochemistry

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	9516-9517
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	31
DOIs	https://doi.org/10.1021/ja049296p
State	Published - Aug 11 2004

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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abstract = "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.",

author = "Hua Deng and Andrzej Lewandowicz and Schramm, {Vern L.} and Robert Callender",

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T1 - Activating the phosphate nucleophile at the catalytic site of purine nucleoside phosphorylase

T2 - A vibrational spectroscopic study

AU - Deng, Hua

AU - Lewandowicz, Andrzej

AU - Schramm, Vern L.

AU - Callender, Robert

PY - 2004/8/11

Y1 - 2004/8/11

N2 - 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.

AB - 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.

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

Abstract

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