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