Spectral and Kinetic Properties of Oxidized Intermediates of Coprinus cinereus Peroxidase.

Andersen, Mikkel Østerheden; Hsuanyu, Yuchiong; Welinder, Karen G.; Schneider, Palle; Dunford, Hugh Brian; Frøystein, Nils Åge; Francis, George W.; Karlsson, Britt

doi:10.3891/acta.chem.scand.45-1080

Cited by 58 publications

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“…For CiP and MPO, it has been observed that compound II is also formed in the presence of sufficient H 2 O 2 via the reduction of compound I by H 2 O 2 itself (39,40). Compound II can, in its turn, react with H 2 O 2 to give compound III, which is believed to be a dead end species and catalytically inactive (41).…”

mentioning

confidence: 99%

Enantioselective Epoxidation and Carbon–Carbon Bond Cleavage Catalyzed by Coprinus cinereus Peroxidase and Myeloperoxidase

Tuynman¹,

Spelberg²,

Kooter³

et al. 2000

Journal of Biological Chemistry

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We demonstrate that myeloperoxidase (MPO) and Coprinus cinereus peroxidase (CiP) catalyze the enantioselective epoxidation of styrene and a number of substituted derivatives with a reasonable enantiomeric excess (up to 80%) and in a moderate yield. Three major differences with respect to the chloroperoxidase from Caldariomyces fumago (CPO) are observed in the reactivity of MPO and CiP toward styrene derivatives. First, in contrast to CPO, MPO and CiP produced the (S)-isomers of the epoxides in enantiomeric excess. Second, for MPO and CiP the H 2 O 2 had to be added very slowly (10 eq in 16 h) to prevent accumulation of catalytically inactive enzyme intermediates. Under these conditions, CPO hardly showed any epoxidizing activity; only with a high influx of H 2 O 2 (300 eq in 1.6 h) was epoxidation observed. Third, both MPO and CiP formed significant amounts of (substituted) benzaldehydes as side products as a consequence of C-␣-C-␤ bond cleavage of the styrene derivatives, whereas for CPO and cytochrome c peroxidase this activity is not observed. C-␣-C-␤ cleavage was the most prominent reaction catalyzed by CiP, whereas with MPO the relative amount of epoxide formed was higher. This is the first report of peroxidases catalyzing both epoxidation reactions and carboncarbon bond cleavage. The results are discussed in terms of mechanisms involving ferryl oxygen transfer and electron transfer, respectively.

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confidence: 99%

Enantioselective Epoxidation and Carbon–Carbon Bond Cleavage Catalyzed by Coprinus cinereus Peroxidase and Myeloperoxidase

Tuynman¹,

Spelberg²,

Kooter³

et al. 2000

Journal of Biological Chemistry

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“…The sample had an RZ value (A 403 /A 280 ) of 2.5. The concentration of ARP was determined using ⑀ 405 of 109 mM Ϫ1 cm Ϫ1 (26). The enzyme was crystallized as described previously (25).…”

Section: Methodsmentioning

confidence: 99%

Direct Binding of Hydroxylamine to the Heme Iron ofArthromyces ramosus Peroxidase

Wariishi¹,

Nonaka²,

Johjima³

et al. 2000

Journal of Biological Chemistry

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The interaction of hydroxylamine (HA) with Arthromyces ramosus peroxidase (ARP) was investigated by kinetic, spectroscopic, and x-ray crystallographic techniques. HA inhibited the reaction of native ARP with H 2 O 2 in a competitive manner. Electron absorption and resonance Raman spectroscopic studies indicated that pentacoordinate high spin species of native ARP are converted to hexacoordinate low spin species upon the addition of HA, strongly suggesting the occurrence of a direct interaction of HA with ARP heme iron. Kinetic analysis exhibited that the apparent dissociation constant is 6.2 mM at pH 7.0 and that only one HA molecule likely binds to the vicinity of the heme. pH dependence of HA binding suggested that the nitrogen atom of HA could be involved in the interaction with the heme iron. X-ray crystallographic analysis of ARP in complex with HA at 2.0 Å resolution revealed that the electron density ascribed to HA is located in the distal pocket between the heme iron and the distal His 56 . HA seems to directly interact with the heme iron but is too far away to interact with Arg 52

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“…Equation 8 describes the dependence of bimolecular constants k 1 on pH. The pK 1 ' value for single protonated ferriperoxidase is equal to 4.9 ± 0.2 [12]. Equation 9 describes the dependence of bimolecular constants k lim on pH.…”

Section: The Optimization Of Hydrogen Peroxide Detection Systems Usinmentioning

confidence: 99%

“…The rCiP, HRP, Cat and hydrogen peroxide solutions were prepared in deionized water and concentrations of these substances were determined spectrophotometrically. For rCiP, HRP, Cat and hydrogen peroxide, the extinction coefficients are ε 405 = 109 mM -1 cm -1 [12], ε 403 = 95 mM -1 cm -1 [16], ε 280 = 150 mM -1 cm -1 [17] and ε 240 = 39.4 M -1 cm -1 [18], respectively. Samples of 1-HP and AR were weighted and dissolved in methanol.…”

Section: Enzymes and Substratesmentioning

confidence: 99%

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Kinetic study of peroxidase-catalyzed oxidation of 1-hydroxypyrene. Development of a nanomolar hydrogen peroxide detection system

Ivanec-Goranina

Kulys

2008

Open Life Sciences

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, respectively. High bimolecular constants and fluorescence quantum yield of 1-HP (0.66) permitted detection as low as 21 nM of H 2 O 2 . To optimize the detection system 1-HP oxidation was modeled at steady-state conditions in the range pH 5.0 to pH 8.0. The 1-HP based detection system was compared with the Amplex Red system. The peroxidase-catalyzed 1-HP oxidation system was used for determination of ozone in the air.

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Spectral and Kinetic Properties of Oxidized Intermediates of Coprinus cinereus Peroxidase.

Cited by 58 publications

References 0 publications

Enantioselective Epoxidation and Carbon–Carbon Bond Cleavage Catalyzed by Coprinus cinereus Peroxidase and Myeloperoxidase

Enantioselective Epoxidation and Carbon–Carbon Bond Cleavage Catalyzed by Coprinus cinereus Peroxidase and Myeloperoxidase

Direct Binding of Hydroxylamine to the Heme Iron ofArthromyces ramosus Peroxidase

Kinetic study of peroxidase-catalyzed oxidation of 1-hydroxypyrene. Development of a nanomolar hydrogen peroxide detection system

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