Effect of pressure on nucleotide binding to yeast alcohol dehydrogenase.
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.
Kidman
Gene
G
Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA.
Northrop
Dexter B
DB
D000042:Absorption; D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000779:Anesthetics, Local / Q000378:metabolism; D019905:Benzyl Alcohol / Q000378:metabolism; D006874:Hydrostatic Pressure; D007700:Kinetics; D008024:Ligands; D008027:Light; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D015003:Yeasts / Q000201:enzymology
D000779:Anesthetics, Local; D008024:Ligands; D009243:NAD; D000426:Alcohol Dehydrogenase; D019905:Benzyl Alcohol