Scavenging of H2O2 and Production of Oxygen by Horseradish Peroxidase

Baker, C. Jacyn; Deahl, Kenneth L.; Domek, John M.; Orlandi, Elizabeth W.

doi:10.1006/abbi.2000.2013

Cited by 40 publications

(20 citation statements)

References 21 publications

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“…A similar effect has been seen with HRP (19,35). The formation of compound III under conditions in which inactivation occurs has been used in some studies with LiP and HRP as evidence that inactivation results from modification of this intermediate (24,43). However, computer simulations of Scheme I (done using the rate constants available for HRP) showed that compound III could be present at high concentrations even though inactivation proceeded from the [compound I⅐H 2 O 2 ] complex (38).…”

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 72%

Reactions of the Class II Peroxidases, Lignin Peroxidase andArthromyces ramosus Peroxidase, with Hydrogen Peroxide

Hiner¹,

Ruiz²,

López³

et al. 2002

Journal of Biological Chemistry

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The reactions of the fungal enzymes Arthromyces ramosus peroxidase (ARP) and Phanerochaete chrysosporium lignin peroxidase (LiP) with hydrogen peroxide (H 2 O 2 ) have been studied. Both enzymes exhibited catalase activity with hyperbolic H 2 O 2 concentration dependence (K m Ϸ 8 -10 mM, k cat Ϸ 1-3 s ؊1 ). The catalase and peroxidase activities of LiP were inhibited within 10 min and those of ARP in 1 h. The inactivation constants were calculated using two independent methods; LiP, k i Ϸ 1 The heme peroxidases have been classified into two distinct groups, termed the animal (found only in animals) and plant (found in plants, fungi, and prokaryotes) superfamilies (1). The plant peroxidases, which share similar overall protein folds and specific features, such as catalytically essential histidine and arginine residues in their active sites, have been subdivided into three classes on the basis of sequence comparison (2, 3). In class I are intracellular enzymes including yeast cytochrome c peroxidase, ascorbate peroxidase (APX) from plants, and bacterial geneduplicated catalase-peroxidases (4). Class III contains the secretory plant peroxidases such as those from horseradish (HRP), barley, or soybean. These peroxidases seem to be biosynthetic enzymes involved in processes such as plant cell wall formation and lignification. Class II consists of the secretory fungal peroxidases such as lignin peroxidase (LiP) from Phanerochaete chrysosporium, manganese peroxidase from the same source, and Coprinus cinereus peroxidase or Arthromyces ramosus peroxidase (ARP), which have been shown to be essentially identical in both sequence and properties (5). The main role of class II peroxidases appears to be the degradation of lignin in wood.All peroxidases studied so far share much the same catalytic cycle that proceeds in three distinct and essentially irreversible steps (6) and is often referred to as the "peroxidase ping-pong." The resting ferric enzyme reacts with H 2 O 2 in a two-electron process to generate the intermediate known as compound I. Compound I is discharged in two sequential single-electron reactions with reducing substrate yielding radical products, which are often highly reactive, and water. The first reduction step results in the formation of another enzyme intermediate, compound II. In the final step compound II is reduced back to ferric peroxidase.The peroxidase ping-pong provides an adequate description of the peroxidase reaction; however, continuing work has revealed some limitations of the basic model. The compound I reduction steps have been shown to consist of reversible substrate binding followed by substrate oxidation (7). The formation and nature of compound I have been studied intensively. Both a neutral peroxidase-peroxide complex and a charged complex (known as compound 0) have been observed (8), and variations have been identified in the electronic structures of the compound Is of different peroxidases (9 -14). Furthermore, certain peroxidases have been found to utilize H 2 O 2 to reduce compoun...

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Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 72%

Reactions of the Class II Peroxidases, Lignin Peroxidase andArthromyces ramosus Peroxidase, with Hydrogen Peroxide

Hiner¹,

Ruiz²,

López³

et al. 2002

Journal of Biological Chemistry

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“…It has been reported that heme peroxidase reacts with H 2 O 2 to form two main ferryl intermediates, compound I (Fe IV =OPorC + ) and compound II (Fe IV =OPor) [1,36] as well as a ferrous-dioxy/ferric-superoxide complex, compound III [1,[36][37][38] , and the irreversibly inactivated form of enzyme, P-670. [37,39] The changes in the Soret band and visible spectra of HRP and metHB upon the addition of H 2 O 2 can be attributed to the formation of compound II, compound III, and P-670. [36,40] On the other hand, compound I is very unstable and rapidly converts to compound II, thus it is difficult to detect under our experimental conditions.…”

Section: Wwwchemeurjorgmentioning

confidence: 99%

Characterization of G‐Quadruplex/Hemin Peroxidase: Substrate Specificity and Inactivation Kinetics

Xiao

Fang

Mei

et al. 2011

Chemistry A European J

104

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Recently, G-quadruplex/hemin (G4/hemin) complexes have been found to exhibit peroxidase activity, and this feature has been extensively exploited for colorimetric detection of various targets. To further understand and characterize this important DNAzyme, its substrate specificity, inactivation mechanism, and kinetics have been examined by comparison with horseradish peroxidase (HRP). G4/hemin DNAzyme exhibits broader substrate specificity and much higher inactivation rate than HRP because of the exposure of the catalytic hemin center. The inactivation of G4/hemin DNAzyme is mainly attributed to the degradation of hemin by H(2)O(2) rather than the destruction of G4. Both the inactivation rate and catalytic oxidation rate of G4/hemin DNAzyme depend on the concentration of H(2)O(2), which suggests that active intermediates formed by G4/hemin and H(2)O(2) are the branch point of catalysis and inactivation. Reducing substrates greatly inhibit the inactivation of G4/hemin DNAzyme by rapidly reacting with the active intermediates. A possible catalytic and inactivation process of G4/hemin has been proposed. These results imply a potential cause for the hemin-mediated cellular injury and provide insightful information for the future application of G4/hemin DNAzyme.

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“…Apart from the peroxidative and oxidative cycles of PODs, a third type of POD activity has been described that mimics the action of catalase; molecular oxygen is produced at the expense of H 2 O 2 in the absence of other reactants (Baker et al 2000). It has also been suggested that when extracellular H 2 O 2 exceeds the supplies of reductants, PODs can display catalase-like activity in vivo and probably are involved in the detoxification of apoplastic H 2 O 2 (Mika et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Effect of heavy metals on root growth and peroxidase activity in barley root tip

et al. 2009

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Scavenging of H2O2 and Production of Oxygen by Horseradish Peroxidase

Cited by 40 publications

References 21 publications

Reactions of the Class II Peroxidases, Lignin Peroxidase andArthromyces ramosus Peroxidase, with Hydrogen Peroxide

Reactions of the Class II Peroxidases, Lignin Peroxidase andArthromyces ramosus Peroxidase, with Hydrogen Peroxide

Characterization of G‐Quadruplex/Hemin Peroxidase: Substrate Specificity and Inactivation Kinetics

Effect of heavy metals on root growth and peroxidase activity in barley root tip

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