The Inactivation and Catalytic Pathways of Horseradish Peroxidase with m-Chloroperoxybenzoic Acid

Rodríguez-López, José Neptuno; Hernández‐Ruíz, Josefa; Garcı́a-Cánovas, Francisco; Thorneley, R. N. F.; Acosta, Manuel; Arnao, Marino B.

doi:10.1074/jbc.272.9.5469

Cited by 86 publications

(74 citation statements)

References 40 publications

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“…Similar phenomena have been reported previously (15,44). Bleaching is commonly seen with heme proteins in their reactions with peroxides and compromise the resolution of active intermediates (45,46). Because of this we were unable to identify an appropriate model to resolve pure species of Compound I with H 2 O 2 .…”

Section: Resultssupporting

confidence: 68%

Prostaglandin Endoperoxide H Synthases

Liu

Seibold

Rieke

et al. 2007

Journal of Biological Chemistry

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The cyclooxygenase (COX) activity of prostaglandin endoperoxide H synthases (PGHSs) converts arachidonic acid and O 2 to prostaglandin G 2 (PGG 2 ). PGHS peroxidase (POX) activity reduces PGG 2 to PGH 2 . The first step in POX catalysis is formation of an oxyferryl heme radical cation (Compound I), which undergoes intramolecular electron transfer forming Intermediate II having an oxyferryl heme and a Tyr-385 radical required for COX catalysis. PGHS POX catalyzes heterolytic cleavage of primary and secondary hydroperoxides much more readily than H 2 O 2 , but the basis for this specificity has been unresolved. Several large amino acids form a hydrophobic "dome" over part of the heme, but when these residues were mutated to alanines there was little effect on Compound I formation from H 2 O 2 or 15-hydroperoxyeicosatetraenoic acid, a surrogate substrate for PGG 2 . Ab initio calculations of heterolytic bond dissociation energies of the peroxyl groups of small peroxides indicated that they are almost the same. Molecular Dynamics simulations suggest that PGG 2 binds the POX site through a peroxyl-iron bond, a hydrogen bond with His-207 and van der Waals interactions involving methylene groups adjoining the carbon bearing the peroxyl group and the protoporphyrin IX. We speculate that these latter interactions, which are not possible with H 2 O 2 , are major contributors to PGHS POX specificity. The distal Gln-203 four residues removed from His-207 have been thought to be essential for Compound I formation. However, Q203V PGHS-1 and PGHS-2 mutants catalyzed heterolytic cleavage of peroxides and exhibited native COX activity. PGHSs are homodimers with each monomer having a POX site and COX site. Cross-talk occurs between the COX sites of adjoining monomers. However, no cross-talk between the POX and COX sites of monomers was detected in a PGHS-2 heterodimer comprised of a Q203R monomer having an inactive POX site and a G533A monomer with an inactive COX site.

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Section: Resultssupporting

confidence: 68%

Prostaglandin Endoperoxide H Synthases

Liu

Seibold

Rieke

et al. 2007

Journal of Biological Chemistry

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“…Following reaction with even very low eq of H 2 O 2 (Ͻ5) the Soret band shifts from 403 to 407 nm prior to bleaching. Production of verdoheme, a product of H 2 O 2 -mediated heme lysis in catalases, peroxidases, and heme oxygenase (52,55,56) is not clearly observed.…”

Section: Circular Dichroism Indicates Intact Secondary Structures Formentioning

confidence: 95%

The Chlorite Dismutase (HemQ) from Staphylococcus aureus Has a Redox-sensitive Heme and Is Associated with the Small Colony Variant Phenotype

Mayfield

Hammer

Kurker

et al. 2013

Journal of Biological Chemistry

112

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“…This was probably because of the inherently unstable nature of this material, which easily loses iron to leave colorless products. The P670 species of APX (17) and HRP-A2 (35) proved equally hard to detect, and that of HRP-C was most stable at 10°C (20).…”

Section: Catalase Activities Of Lip and Arp-bothmentioning

confidence: 99%

“…In the case of HRP, the complex between compound I and peroxide ([compound I⅐H 2 O 2 ]) has been identified unambiguously as the pivotal point connecting the three simultaneous pathways (19,20). Thus, the peroxidase ping-pong mechanism can be replaced by an alternative catalytic cycle (Scheme I) when no substrate other than H 2 O 2 is present.…”

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confidence: 99%

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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The Inactivation and Catalytic Pathways of Horseradish Peroxidase with m-Chloroperoxybenzoic Acid

Cited by 86 publications

References 40 publications

Prostaglandin Endoperoxide H Synthases

Prostaglandin Endoperoxide H Synthases

The Chlorite Dismutase (HemQ) from Staphylococcus aureus Has a Redox-sensitive Heme and Is Associated with the Small Colony Variant Phenotype

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

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