Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2

Hernández‐Ruíz, Josefa; Arnao, Marino B.; Hiner, Alexander N.P.; Garcı́a-Cánovas, Francisco; Acosta, Manuel

doi:10.1042/bj3540107

Cited by 124 publications

(66 citation statements)

References 39 publications

(71 reference statements)

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“…A global partition ratio may be defined: r ϭ r cat ϩ r coIII ϭ (k 3 ϩ k 4 )/k i . In the case of HRP-C, it has been shown previously that r cat Ͼ Ͼ r coIII (18,30), and thus r Ϸ r cat . The data obtained in the present study suggest that this relationship also applies to LiP and ARP.…”

Section: Methodsmentioning

confidence: 99%

“…These data could be fitted using the MichaelisMenten equation, which in this case takes the following form (18),…”

Section: Methodsmentioning

confidence: 99%

“…the infinite product of the catalase reaction) confirmed that LiP lost activity much more rapidly than ARP. The values of the partition ratios (r), obtained from the slopes of the straight line fits to plots of [O 2 ] ϱ against [peroxidase] (not shown) (18) indicated that LiP (r ϭ 155 Ϯ 25) was more sensitive to inactivation by H 2 O 2 than ARP (r ϭ 620 Ϯ 60). Additionally, using the relationship r Ϸ k 3 /k i (18) (see Scheme I), it was calculated that the inactivation constant of LiP (k i ϭ (18.5 Ϯ 2.3) ϫ 10 Ϫ3 s Ϫ1 ) was 10-fold higher than for ARP (k i ϭ (1.85 Ϯ 0.18) ϫ 10 Ϫ3 s Ϫ1 ).…”

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 99%

“…In both of these cases it was found that H 2 O 2 acted as a mechanism-based (suicide) inactivator (44,45); however, important differences were detected between these enzymes. HRP showed considerable catalase activity (18,35,38), and a large stoichiometric excess of H 2 O 2 was required for inactivation (19). From the data that were amassed we formulated a reaction model for HRP plus H 2 O 2 (Scheme I).…”

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 99%

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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: Methodsmentioning

confidence: 99%

“…These data could be fitted using the MichaelisMenten equation, which in this case takes the following form (18),…”

Section: Methodsmentioning

confidence: 99%

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 99%

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 99%

See 2 more Smart Citations

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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“…H 2 O 2 concentrations were determined spectrophotometrically using 43.6 M -1 cm -1 as the extinction coefficient [11]. Samples were exposed to the relevant H 2 O 2 concentration for 30 min at 25 o C in a temperaturecontrolled waterbath.…”

mentioning

confidence: 99%

Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide

Ryan

Ó’Fágáin

2007

Biochimie

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Zinc in Soils and Crop Nutrition

Sadeghzadeh¹,

Rengel

2011

The Molecular and Physiological Basis of Nutrient Use Efficiency in Crops

143

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Zinc (Zn) is an essential micronutrient and has particular physiological functions in all living systems, such as the maintenance of structural and functional integrity of biological membranes and facilitation of protein synthesis and gene expression. Among all metals, Zn is needed by the largest number of proteins. Zinc-binding proteins make up nearly 10 % of the proteomes in eukaryotic cells, and 36% of the eukaryotic Zn-proteins are involved in gene expression (Andreini et al., 2006, J. Proteome Res. 5: 3173-3178). Tolerance to environmental stress conditions has a high requirement for Zn to regulate and maintain the expression of genes needed to protect cells from the detrimental effects of stress

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Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2

Cited by 124 publications

References 39 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

Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide

Zinc in Soils and Crop Nutrition

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