Monomer formation and functioning of p-hydroxybenzoate hydroxylase in reverse micelles and dimethylsulfoxide-water mixtures.

E.V. Kudryashova, A.J.W.G. Visser, J.W.H. van Berkel

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

It has previously been postulated that the dimeric form of the flavoprotein p-hydroxybenzoate hydroxylase (PHBH) is important for catalysis. Here it is demonstrated that the monomeric form of PHBH is active. In a water/AOT/isooctane reverse micellar system, the function of the monomeric and dimeric forms of PHBH could be observed separately by varying the size of the micelles. A considerable decrease in the K
Original languageEnglish
Pages (from-to)413-419
JournalChemBioChem
Volume9
DOIs
Publication statusPublished - 2008

Fingerprint

Dive into the research topics of 'Monomer formation and functioning of p-hydroxybenzoate hydroxylase in reverse micelles and dimethylsulfoxide-water mixtures.'. Together they form a unique fingerprint.

Cite this