Effect of pressure on nucleotide binding to yeast alcohol dehydrogenase

被引：3

作者：

Kidman, G ^{[1
]}

Northrop, DB ^{[1
]}

机构：

[1] Univ Wisconsin, Sch Pharm, Div Pharmaceut Sci, Madison, WI 53705 USA

来源：

PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 05期

关键词：

D O I：

10.2174/0929866054395293

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 enzyme-nucleotide 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.

引用

页码：495 / 497

页数：3

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