Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis
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منابع مشابه
Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis.
The vanadium-dependent chloroperoxidase from Curvularia inaequalis is a stable and efficient biocatalyst for the hydroxyhalogenation of a broad range of alkenes into halohydrins. Up to 1 200 000 TON with 69 s-1 TOF were observed for the biocatalyst. A bienzymatic cascade to yield epoxides as reaction products is presented.
متن کاملX-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis belongs to a class of vanadium enzymes that oxidize halides in the presence of hydrogen peroxide to the corresponding hypohalous acids. The 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center. Azide coordinates directly to the metal center, resulting ...
متن کاملThe stability and steady-state kinetics of vanadium chloroperoxidase from the fungus Curvularia inaequalis.
In this article we report on the steady-state kinetics of the chlorination and the stability of the vanadium chloroperoxidase from the fungus Curvularia inaequalis. The data show that the kinetics of this enzyme resemble that of the vanadium bromoperoxidase from the seaweed Ascophyllum nodosum. At low pH, chloride inhibited the enzyme, but the inhibition was of a dual nature. At pH 4.1 a mixed ...
متن کاملInhibition of vanadium chloroperoxidase from the fungus Curvularia inaequalis by hydroxylamine, hydrazine and azide and inactivation by phosphate.
The first detailed inhibition study of recombinant vanadium chloroperoxidase (rVCPO) using hydroxylamine, hydrazine and azide has been carried out. Hydroxylamine inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant K(ic) and the uncompetitive inhibition constant K(iu) see are 40 and 80 microM, respectively. The kinetic data suggest that rVCPO may form a hyd...
متن کاملHeterologous Expression of the Vanadium-containing Chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and Site-directed Mutagenesis of the Active Site Residues
The vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis is heterologously expressed to high levels in the yeast Saccharomyces cerevisiae. Characterization of the recombinant enzyme reveals that this behaves very similar to the native chloroperoxidase. Site-directed mutagenesis is performed on four highly conserved active site residues to examine their role in catalysis. W...
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ژورنال
عنوان ژورنال: Chemical Communications
سال: 2017
ISSN: 1359-7345,1364-548X
DOI: 10.1039/c7cc03368k