Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase.

DePillis, Gia D.; Sishta, Bhavini P.; Mauk, A. Grant; Montellano, Paul R. Ortiz de

doi:10.1016/s0021-9258(18)55002-x

Cited by 69 publications

(37 citation statements)

References 30 publications

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“…The non-natural DFSM-facilitated P450-H 2 O 2 system described above mainly catalyzes various per-oxygenation reactions, including epoxidation, hydroxylation, and sulfoxidation [66,[92][93][94][95]. Interestingly, the oxidation of guaiacol, a classical substrate of peroxidases [141][142][143][144], catalyzed by the DFSM-facilitated P450BM3-H 2 O 2 system yielded demethylated catechol as a major product, suggesting it mainly functioned as a peroxygenase but not as a peroxidase [94]. After carefully analyzing the catalytic mechanism of the potential competitive oxidation pathways in the DFSM-facilitated P450BM3-H 2 O 2 system, Ma et al hypothesized that mutation of redox-sensitive residues may enable switching of peroxygenase activity to peroxidase activity [145].…”

Section: Switching Peroxidase Activity Of the Dfsm-facilitated P450 P...mentioning

confidence: 99%

A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective

Fan

Jiang

et al. 2022

Antioxidants

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Cytochrome P450 monooxygenases (P450s) are promising versatile oxidative biocatalysts. However, the practical use of P450s in vitro is limited by their dependence on the co-enzyme NAD(P)H and the complex electron transport system. Using H2O2 simplifies the catalytic cycle of P450s; however, most P450s are inactive in the presence of H2O2. By mimicking the molecular structure and catalytic mechanism of natural peroxygenases and peroxidases, an artificial P450 peroxygenase system has been designed with the assistance of a dual-functional small molecule (DFSM). DFSMs, such as N-(ω-imidazolyl fatty acyl)-l-amino acids, use an acyl amino acid as an anchoring group to bind the enzyme, and the imidazolyl group at the other end functions as a general acid-base catalyst in the activation of H2O2. In combination with protein engineering, the DFSM-facilitated P450 peroxygenase system has been used in various oxidation reactions of non-native substrates, such as alkene epoxidation, thioanisole sulfoxidation, and alkanes and aromatic hydroxylation, which showed unique activities and selectivity. Moreover, the DFSM-facilitated P450 peroxygenase system can switch to the peroxidase mode by mechanism-guided protein engineering. In this short review, the design, mechanism, evolution, application, and perspective of these novel non-natural P450 peroxygenases for the oxidation of non-native substrates are discussed.

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Section: Switching Peroxidase Activity Of the Dfsm-facilitated P450 P...mentioning

confidence: 99%

A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective

Fan

Jiang

et al. 2022

Antioxidants

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“…Measurements were performed using the following substrate concentrations: 0.1 mM for sinapic and ferulic acids; 1mM for ABTS, gallic acid, and 2,6-DMP; 5 mM for guaiacol; and 10 mM for catechol. The molar extinction coefficients were 740 cm −1 •M −1 at 410 nm for catechol [35], 29,500 cm −1 •M −1 at 436 nm for ABTS [13], 35,645 cm −1 •M −1 at 470 nm for 2,6-DMP [36], 26,600 cm −1 •M −1 at 470 nm for guaiacol [37], 4610 cm −1 •M −1 at 385 nm for gallic acid [38], 14,640 cm −1 •M −1 at 306 nm for sinapic acid [39], and 12,940 cm −1 •M −1 at 314 nm for ferulic acid [33]. All measurements were performed in triplicate.…”

Section: Laccase Characterizationmentioning

confidence: 99%

Purification and Characterization of Two Novel Laccases from Peniophora lycii

Glazunova

Moiseenko

Savinova

et al. 2020

JoF

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Although, currently, more than 100 laccases have been purified from basidiomycete fungi, the majority of these laccases were obtained from fungi of the Polyporales order, and only scarce data are available about the laccases from other fungi. In this article, laccase production by the white-rot basidiomycete fungus Peniophora lycii, belonging to the Russulales order, was investigated. It was shown that, under copper induction, this fungus secreted three different laccase isozymes. Two laccase isozymes—Lac5 and LacA—were purified and their corresponding nucleotide sequences were determined. Both purified laccases were relatively thermostable with periods of half-life at 70 °C of 10 and 8 min for Lac5 and LacA, respectively. The laccases demonstrated the highest activity toward ABTS (97 U·mg−1 for Lac5 and 121 U·mg−1 for LacA at pH 4.5); Lac5 demonstrated the lowest activity toward 2,6-DMP (2.5 U·mg−1 at pH 4.5), while LacA demonstrated this towards gallic acid (1.4 U·mg−1 at pH 4.5). Both Lac5 and LacA were able to efficiently decolorize such dyes as RBBR and Bromcresol Green. Additionally, phylogenetic relationships among laccases of Peniophora spp. were reconstructed, and groups of orthologous genes were determined. Based on these groups, all currently available data about laccases of Peniophora spp. were systematized.

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“…In order to optimize the experimental conditions and to avoid possible catalyst destruction by excess H 2 O 2 , kinetic experiments were performed to determine the optimal H 2 O 2 concentration. Immediately after addition of H 2 O 2 to guaiacol solution containing rHSA(wt)–heme, the absorbance of the resulting product ( λ max =470 nm) gradually increased 15. 16 The initial rates ( v 0 ) for the guaiacol oxidation at various concentrations of H 2 O 2 (0–14.0 m M ) and fixed guaiacol concentration (0.5 m M ) are shown in Figure S1 in the Supporting Information.…”

Section: Steady‐state Kinetic Parameters For Guaiacol Oxidation By H2o2 With Rhsa(mutant)–heme Complex In 50 MM Pb Solution (Ph 70) At 20mentioning

confidence: 99%

“…Immediately after addition of H 2 O 2 to guaiacol solution containing rHSA(wt)-heme, the absorbance of the resulting product (l max = 470 nm) gradually increased. [15,16] The initial rates (v 0 ) for the guaiacol oxidation at various concentrations of H 2 O 2 (0-14.0 mm) and fixed guaiacol concentration (0.5 mm) are shown in Figure S1 in the Supporting Information. The maximum of the curve corresponds to the optimal H 2 O 2 concentration.…”

mentioning

confidence: 99%

Human Serum Albumin‐Based Peroxidase Having an Iron Protoporphyrin IX in Artificial Heme Pocket

Watanabe

Ishikawa

Komatsu

2012

Chemistry An Asian Journal

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Cooking up enzymes: Iron protoporphyrin IX (heme) is bound within a hydrophobic cavity in subdomain IB of human serum albumin (HSA). Site-specific mutations to introduce proximal and distal histidines into the heme pocket of HSA conferred a peroxidase activity to the prosthetic heme group. The catalytic activity of the recombinant HSA(mutant)-heme complex for guaiacol oxidation is 17-fold higher than that of HSA(wild type)-heme.

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Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase.

Cited by 69 publications

References 30 publications

A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective

A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective

Purification and Characterization of Two Novel Laccases from Peniophora lycii

Human Serum Albumin‐Based Peroxidase Having an Iron Protoporphyrin IX in Artificial Heme Pocket

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