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

Research output: Contribution to journalArticle

37 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)9516-9517
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number31
DOIs
StatePublished - Aug 11 2004

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Purine-Nucleoside Phosphorylase
Nucleophiles
Fourier Transform Infrared Spectroscopy
Catalytic Domain
Phosphates
Enzymes
Nucleosides

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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AU - Callender, Robert

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