Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis

Sheffield, D. J.; Harry, Tim R; Smith, A. J.; Rogers, Lyndon J.

doi:10.1016/0031-9422(92)80099-z

Cited by 59 publications

(47 citation statements)

References 32 publications

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“…The stability studies showed that the enzyme was stable to high temperatures, with reversible activity loss at a tempeature of 90°C. Loss of haloperoxidase activity at 90°C followed by reactivation at 20°C was consistent with the results of Sheffield et al [12]. In the presence of excess sodium orthovanadate (10 mM), activity loss was not observed at 80°C.…”

Section: Resultssupporting

confidence: 92%

“…The use of the C officinalis enzyme for biotransformations has been demonstrated by its ability to carry out regiospecific halogenations of cinnamyl substrates [ 10]. Regiospecific halogenation and typical high stability towards oxidants, organic solvents [11] and temperature [12] make vanadium-dependent haloperoxidases interesting catalysts for use in future biotransformations.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

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Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis

Rush¹,

Willetts²,

Davies³

et al. 1995

FEBS Letters

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understanding of the multimeric arrangements of the protein subunits and the role of vanadium in the catalytic action. One property of the vanadium cofactor in haloperoxidases is that it can be removed at low pH in the presence of EDTA, rendering the enzyme inactive. Incubation of the enzyme at neutral pH with vanadate restores activity. This has led to the suggestion, which is confirmed by spectroscopic studies, that the vanadium is in the valance state 5+ (3d °) [14].

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Section: Resultssupporting

confidence: 92%

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis

Rush¹,

Willetts²,

Davies³

et al. 1995

FEBS Letters

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“…Examination A common feature associated with most vanadium-type haloperoxidases is their high thermostability (6,11,30), although with exceptions for example the vanadium bromoperoxidase from Ceramium rubrum (12). CvCPO is known to still be active at temperatures exceeding 80°C, although activity begins to drop after this point (6).…”

Section: Sds-polyacrylamide Gel Electrophoresis Analysis Of Purified mentioning

confidence: 99%

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Barnett

Hemrika

Dekker

et al. 1998

Journal of Biological Chemistry

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Here we describe the isolation, purification, and basic kinetic parameters of a vanadium type chloroperoxidase from the hyphomycete fungus Embellisia didymospora. The enzyme proved to possess similar high substrate affinities, a K m of 5 M for a bromide, 1.2 mM for a chloride, and 60 M for a hydrogen peroxide, as those of the vanadium chloroperoxidase from Curvularia inaequalis, although with lower turnover rates for both Cl ؊ and Br ؊ . Substrate bromide was also found to inhibit the enzyme, a feature subsequently also noted for the chloroperoxidase from C. inaequalis. The gene encoding this enzyme was identified using DNA Southern blotting techniques and subsequently isolated and sequenced. A comparison is made between this vanadium chloroperoxidase and that of the fungus C. inaequalis both kinetically and at the sequence level. At the primary structural level the two chloroperoxidases share 68% identity, with conservation of all active site residues.

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“…Subsequently vanadium dependent haloperoxidases were identified in a number of different types of algae (Vollenbroek et aL, 1995) ;~,~ 1998 International Union of Crystallography Printed in Great Britain -all rights reserved and also fungi (Van Schijndel et aL, 1993) and lichen . The vanadium-dependent bromoperoxidase from C. officinalis has been well characterized (Sheffield et aL, 1993). It is thermostable retaining activity at 363 K and is stable in organic solvents such as ethanol, propanol and acetone (Rush et aL, 1995).…”

Section: Monochlorodimedonementioning

confidence: 99%

Preliminary X-ray analysis of a new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis

Brindley

Dalby

Isupov

et al. 1998

Acta Crystallogr D Biol Cryst

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A new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis has been obtained. The crystals exhibit a 'teardrop' morphology and are grown from 2 M ammonium dihydrogen phosphate pH 5 and diffract to beyond 1.7,4, resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9, c = 178.19 A, a = fl = y = 90 °. A 2.3 ,,% resolution native data set has been collected at the Hamburg Synchrotron. A mercury derivative data set has also been collected, and the heavy-atom positions have been determined. The self-rotation function and the positions of the heavy atoms are consistent with the molecule being a dodecamer with local 23 symmetry.

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Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis

Cited by 59 publications

References 32 publications

Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis

Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Preliminary X-ray analysis of a new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis

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