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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Effect of Pressure on Nucleotide Binding to Yeast Alcohol Dehydrogenase

Author(s): Gene Kidman and Dexter B. Northrop

Volume 12, Issue 5, 2005

Page: [495 - 497] Pages: 3

DOI: 10.2174/0929866054395293

Price: $65

Abstract

Binding of reduced nicotinamide adenine dinucleotide to yeast alcohol dehydrogenase results in a hypsochromic shift of its absorbance maximum at 340 nm. Application of high hydrostatic pressure to the enzymenucleotide complex returns the absorbance maximum to longer wavelengths. This pressure-dependent bathochromic shift validates one of two assignments on the effects of pressure on the kinetics of the enzymatic oxidation of benzyl alcohol, namely the protein-ligand conformational change of the capturing form of enzyme.

Keywords: hypsochromic shift, bathochromic shift, hydrostatic pressure, yeast alcohol dehydrogenase, nadh, cycloamylose

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