The importance of monopole-monopole and monopole-dipole interactions on the binding of NADPH and NADPH analogues to p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens effects of pH and ionic strength

NADPH binding to p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens is found to be strongly dependent on pH and ionic strength. In the ionic strength range of 0.02-0.15 M, optimal NADPH binding is observed at a pH value of 6.4. Extrapolation of the dissociation constants to infinite ionic st...

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Veröffentlicht in:	European journal of biochemistry 1984-03, Vol.139 (3), p.637-644
Hauptverfasser:	WIJNANDS, R. A, VAN DER ZEE, J, VAN LEEUWEN, J, VAN BERKEL, J. H, MÜLLER, F
Format:	Artikel
Sprache:	eng
Schlagworte:	4-Hydroxybenzoate-3-Monooxygenase - metabolism Analytical, structural and metabolic biochemistry Binding, Competitive Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Mixed Function Oxygenases - metabolism Models, Chemical NADP - analogs & derivatives NADP - metabolism Osmolar Concentration Oxidoreductases Protein Binding Pseudomonas fluorescens - enzymology Substrate Specificity Temperature
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