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

doi:10.1002/cbic.200700267

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 Journal › Article › Academic › peer-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 language	English
Pages (from-to)	413-419
Journal	ChemBioChem
Volume	9
DOIs	https://doi.org/10.1002/cbic.200700267
Publication status	Published - 2008

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 6 Clean Water and Sanitation

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10.1002/cbic.200700267

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

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",

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year = "2008",

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journal = "ChemBioChem",

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AU - Kudryashova, E.V.

AU - Visser, A.J.W.G.

AU - van Berkel, J.W.H.

PY - 2008

Y1 - 2008

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AB - 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

U2 - 10.1002/cbic.200700267

DO - 10.1002/cbic.200700267

M3 - Article

SN - 1439-4227

VL - 9

SP - 413

EP - 419

JO - ChemBioChem

JF - ChemBioChem

ER -

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

Abstract

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