Results 261 to 270 of about 61,259 (301)

Crystal structure of recombinant pea cytosolic ascorbate peroxidase

Biochemistry, 1995
The crystal structure of recombinant pea cytosolic ascorbate peroxidase has been refined to an R = 0.19 for data between 8.0 and 2.2 A resolution and magnitude of F > or = 2 sigma(magnitude of F). The refined model consists of four ascorbate peroxidase monomers consisting of 249 residues per monomer assembled into two homodimers, with one heme group ...
W R, Patterson, T L, Poulos
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Peroxidase-Catalyzed Oxidation of Ascorbate Structural, Spectroscopic and Mechanistic Correlations in Ascorbate Peroxidase

2000
Ascorbate-dependent peroxidase activity was first reported in 1979 (Groden and Beck, 1979; Kelly and Latzko, 1979) and ascorbate peroxidase (APX) is, therefore, a relative newcomer to the peroxidase field--horseradish (HRP) and cytochrome c (CcP) peroxidases were, for example, first identified in 1903 (Bach and Chodat, 1903) and 1940 (Altschul et al ...
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Catalytic Oxidation of p-Cresol by Ascorbate Peroxidase

Archives of Biochemistry and Biophysics, 2000
Transient and steady state kinetics, together with a range of chromatographic and spectroscopic techniques, have been used to establish the mechanism and the products of the H(2)O(2)-dependent oxidation of p-cresol by ascorbate peroxidase (APX). HPLC, GC-MS, and NMR analyses are consistent with the formation of 2, 2'-dihydroxy-5,5'-dimethylbiphenyl (II)
Celik, A, Cullis, PM, Lloyd Raven E
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Ascorbate peroxidase‐related (APx‐R) is a new heme‐containing protein functionally associated with ascorbate peroxidase but evolutionarily divergent

New Phytologist, 2011
• Peroxidases are involved in several important processes, such as development and responses to environmental cues. In higher plants, most peroxidases are encoded by large, multigenic families that mainly originated from gene and chromosomal duplications.
Fernanda, Lazzarotto, Felipe Karam, Teixeira, Silvia Barcelos, Rosa, Christophe, Dunand, Claudia Lemelle, Fernandes, Adilton, de Vasconcelos Fontenele, Joaquim Albenisio Gomes, Silveira, Hugo, Verli, Rogério, Margis, Marcia, Margis-Pinheiro   +9 more
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Effectiveness of ascorbate and ascorbate peroxidase in promoting nitrogen fixation in model systems

Phytochemistry, 1999
Ascorbate and ascorbate peroxidase are important antioxidants that are abundant in N2-fixing legume root nodules. Antioxidants are especially critical in root nodules because leghemoglobin, which is present at high concentrations in nodules, is prone to autoxidation and production of activated oxygen species such as O2.- and H2O2.
E J, Ross, S B, Kramer, D A, Dalton
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Distribution of cytosolic ascorbate peroxidase in Angiosperms

Giornale botanico italiano, 1996
Abstract Over 80 Angiosperms have been screened for cytosolic ascorbate peroxidase by means of native-polyacrylamide gel electrophoresis techniques. The results of our analysis show that the presence of a single cytosolic ascorbate peroxidase form is the most common case in the Angiosperms investigated when seedlings or young tissues are analized. This
PACIOLLA, Costantino, De Gara L, DE TULLIO, Mario, Arrigoni O.   +3 more
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Physiological function and regulation of ascorbate peroxidase isoforms

Journal of Experimental Botany
AbstractAscorbate peroxidase (APX) reduces H2O2 to H2O by utilizing ascorbate as a specific electron donor and constitutes the ascorbate–glutathione cycle in organelles of plants including chloroplasts, cytosol, mitochondria, and peroxisomes. It has been almost 40 years since APX was discovered as an important plant-specific H2O2-scavenging enzyme ...
Kazuya Yoshimura, Takahiro Ishikawa
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Defining substrate specificity and catalytic mechanism in ascorbate peroxidase

Biochemical Society Symposia, 2004
Haem peroxidases catalyse the H2O2-dependent oxidation of a variety of, usually organic, substrates. Mechanistically, these enzymes are very well characterized: they share a common catalytic cycle that involves formation of a two-electron oxidized intermediate (Compound I) followed by reduction of Compound I by substrate.
Emma L, Raven, Latesh, Lad, Katherine H, Sharp, Martin, Mewies, Peter C E, Moody   +4 more
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Ascorbate peroxidase – a hydrogen peroxide‐scavenging enzyme in plants

Physiologia Plantarum, 1992
Ascorbate peroxidase is a hydrogen peroxide‐scavenging enzyme that is specific to plants and algae and is indispensable to protect chloroplasts and other cell constituents from damage by hydrogen peroxide and hydroxyl radicals produced from it. In this review, first, the participation of ascorbate peroxidase in the scavenging of hydrogen peroxide in ...
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Ascorbate guided conversion of hydrogen peroxide to hydroxyl radical on goethite

Applied Catalysis B: Environmental, 2021
Lizhi Zhang
exaly