A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide

Arnao, Marino B.; Acosta, Manuel; Rı́o, José Antonio del; Varón, R.; Garcı́a-Cánovas, Francisco

doi:10.1016/0167-4838(90)90120-5

Cited by 263 publications

(175 citation statements)

References 21 publications

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“…This happens in the absence of reductant substrates or with a high oxidant/reductant ratio (2,3,6,7,11,24,(27)(28)(29).…”

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

“…reacts with a great variety of reductant substrates, using H20 2 as oxidizing agent (1). However, in the absence of reductant substrates, an excess of H20 2 leads to inactivation of the enzyme, the H~02, in this case, acting as a suicide substrate of peroxidase (2,3). It has been proposed that this inactivation process takes place at the level of Compound I, the first active intermediate form of peroxidase, and that it is related with the appearance of an inactive compound called P-670 (2,4).…”

Section: Introductionmentioning

confidence: 99%

“…However, in the absence of reductant substrates, an excess of H20 2 leads to inactivation of the enzyme, the H~02, in this case, acting as a suicide substrate of peroxidase (2,3). It has been proposed that this inactivation process takes place at the level of Compound I, the first active intermediate form of peroxidase, and that it is related with the appearance of an inactive compound called P-670 (2,4). Other hydroperoxides, such as hydroxymethyl hydroperoxide (5), m-nitroperoxybenzoic acid (4), mcbloroperoxybenzoic acid (3) and the skatole hydroperoxide derived from indolyl-3-acetic acid (4,6) also inactivate the enzyme in a similar way.…”

Section: Introductionmentioning

confidence: 99%

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Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

1996

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SUMMARYHorseradish peroxidase reacts with H202 and other hydroperoxides to form Compound I, the first active enzymatic form. m-Chloroperoxybenzoic acid, a xenobiotic hydroperoxide, acts as an oxidant substrate of horseradish peroxidase. However, this hydroperoxide is also a powerful inactivator of the enzyme and in this sense is more effective than H202. The coupled reductant substrates used in the peroxidatic reaction protect the enzyme from the inactivating process.A reaction mechanism is proposed with two competitive routes: one catalytic and one inactivating. Using a kinetic approach, the ratio between the hydroperoxide and the reductant substrate appears to be a decisive factor in the catalytic turnover of the enzyme.The role of the reductant substrates in protecting the enzyme, and the physiological and biotechnological implications of this process are discussed.

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“…This happens in the absence of reductant substrates or with a high oxidant/reductant ratio (2,3,6,7,11,24,(27)(28)(29).…”

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

1996

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“…However, this was verified with a timedependent test in this study. Less H 2 O 2 would be a limiting condition whereas, excessive H 2 O 2 concentrations lead to the deactivation of the enzymes due to the formation of Compound III, an enzymatic state in which the enzyme does not recover and is considered to be deactivated (Arnao et al, 1990). After 3 h the reaction was halted by the addition of catalase in a 1:1 molar equivalent ratio with the substrate to decompose the H 2 O 2 .…”

Section: Batch Testsmentioning

confidence: 99%

Optimisation of soybean peroxidase treatment of 2, 4-dichlorophenol

Kennedy¹,

Alemany²,

Warith³

2002

WSA

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In the presence of hydrogen peroxide (H 2 O 2 ), peroxidase enzymes (PE) catalyse the oxidation of various chlorinated phenols to free radicals, which then combine to form insoluble polymers that precipitate out of solution. This study systematically characterises the treatment of 2,4-dichlorophenol (2,4-DCP) using soybean peroxidase (SBP) as an oxidising catalyst. The effects of pH, SBP concentration, polyethylene glycol (PEG) additive and initial chlorophenol concentration on 2,4-DCP treatments are reported. Optimum pH for removal of 2,4-DCP without PEG was pH 8.2. The pH operating range of SBP was from 2.5 to 9.4 which is wider than reported for horseradish peroxidase (HRP). A general equation is presented that describes the units of SBP required (without PEG) to treat a given amount of 2,4-DCP at the optimum pH of 8.2. Addition of PEG increased the effectiveness of SBP by factors of 10 and 50 for PEG-3350 and PEG-8000 respectively. A new pH optimum of 6.2 was also found when SBP was used with PEG. Batch and semi -batch enzyme delivery has also been identified as a crucial parameter for the SBP treatment process. The most effective addition scheme was based on five equal concentrations of SBP and H 2 O 2 over 15 min and 30 min intervals respectively compared to a single batch addition. This protocol was the most effective as it took advantage of limiting the amount of SBP and H 2 O 2 available at each step. This reduces the possible chance of SBP inactivation by excessive H 2 O 2 when using a single batch concentration. Average 2,4-DCP removals achieved were 83.5%, 75.5% and 71.5% for 100, 200 and 300 mg/l 2,4-DCP concentrations respectively compared to 62%, 52% and 58% for the single batch addition control.

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“…K , an inhibitor-binding constant, were obtained from the corresponding fitting of the data by a linear regression model [63].…”

Section: Kinetics Of Inactivation By H 2 Omentioning

confidence: 99%

Steady-state kinetics of <i>Roystonea regia</i> palm tree peroxidase

Zamorano¹,

Cuadrado²,

Galende³

et al. 2012

JBPC

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A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide

Cited by 263 publications

References 21 publications

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

Optimisation of soybean peroxidase treatment of 2, 4-dichlorophenol

Steady-state kinetics of <i>Roystonea regia</i> palm tree peroxidase

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A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide

Cited by 263 publications

References 21 publications

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

Optimisation of soybean peroxidase treatment of 2, 4-dichlorophenol

Steady-state kinetics of &lt;i&gt;Roystonea regia&lt;/i&gt; palm tree peroxidase

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Steady-state kinetics of <i>Roystonea regia</i> palm tree peroxidase