Isolation and Characterization of Five Neutral Isoenzymes of Horseradish Peroxidase1

Aibara, Shigeo; Yamashita, Honami; Mori, Eigo; Kato, Masanori; Morita, Yuhei

doi:10.1093/oxfordjournals.jbchem.a133961

Cited by 111 publications

(60 citation statements)

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“…HRPC was also obtained from Sigma Aldrich and was used without any further purification. Protein concentration of HRPC was determined spectrophotometerically by measuring absorbance at 403 nm (⑀ 403 ϭ 102,000 M Ϫ1 cm Ϫ1 ) (31). mtCP was prepared as described in Bertrand et al (2).…”

Section: Methodsmentioning

confidence: 99%

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Pierattelli

Banci

Eady

et al. 2004

Journal of Biological Chemistry

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There is an urgent need to understand the mechanism of activation of the frontline anti-tuberculosis drug isoniazid by the Mycobacterium tuberculosis catalase-peroxidase. To address this, a combination of NMR spectroscopic, biochemical, and computational methods have been used to obtain a model of the frontline anti-tuberculosis drug isoniazid bound to the active site of the class III peroxidase, horseradish peroxidase C. This information has been used in combination with the new crystal structure of the M. tuberculosis catalase-peroxidase to predict the mode of INH binding across the class I heme peroxidase family. An enzyme-catalyzed mechanism for INH activation is proposed that brings together structural, functional, and spectroscopic data from a variety of sources. Collectively, the information not only provides a molecular basis for understanding INH activation by the M. tuberculosis catalase-peroxidase but also establishes a new conceptual framework for testing hypotheses regarding the enzyme-catalyzed turnover of this compound in a number of heme peroxidases.

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Section: Methodsmentioning

confidence: 99%

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Pierattelli

Banci

Eady

et al. 2004

Journal of Biological Chemistry

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“…But in this case, other metabolites can be formed from cyanide (CN -) or azide (N 3 -), such as cyanyl (CN • ) or azidyl (N 3 • ) radicals respectively, which can interfere with ROS measurement [32]. Moreover, cyanide and azide are well know inhibitors of cytochrome C oxidase (ETC complex IV) and of horseradish peroxidase, often used in ROS measurement methods [33].…”

Section: Methods For Ros Measurementmentioning

confidence: 99%

Determination of mitochondrial reactive oxygen species: methodological aspects

Batandier

Fontaine

Kériel

et al. 2002

J Cellular Molecular Medi

138

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The generation of Reactive Oxygen Species (ROS) as by-products in mitochondria Electron Transport Chain (ETC) has long been admitted as the cost of aerobic energy metabolism with oxidative damages as consequence. The purpose of this methodological review is to present some of the most widespread methods of ROS generation and to underline the limitations as well as some problems, identified with some experiments as examples, in the interpretation of such results. There is now no doubt that besides their pejorative role, ROS are involved in a variety of cellular processes for the continuous adaptation of the cell to its environment. Because ROS metabolism is a complex area (low production, instability of species, efficient antioxidant defense system, several places of production…) bias, variances and limitations in ROS measurements must be recognized in order to avoid artefactual conclusions, and especially to improve our understanding of physiological and pathophysiological mechanisms of such phenomenon.

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“…Horseradish isoperoxidases HRP A and HRP C have been analyzed for Ca2+ content by Haschke and Friedhoff [37], HRP BI, HRP B2, HRP B3, HRP C1 and HRP C2 by Aibara et al [38] by atomic absorption spectrometry. All contain two Ca2+ per molecule.…”

Section: + In Plant Peroxidasesmentioning

confidence: 99%

Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase

Welinder

1985

Eur J Biochem

165

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The amino acid sequences of the 51% different horseradish peroxidase HRP C and turnip peroxidase TP 7 have previously been completed by us, but the three-dimensional structures are unknown. Recently the amino acid sequence and the crystal structure of yeast cytochrome c peroxidase have appeared. The three known apoperoxidases consist of 300 & 8 amino acid residues. The sequences have now been aligned and show 18% and 16% identity only, between the yeast peroxidase and plant peroxidase HRP C and TP 7, respectively. We show that different structural tests all support similar protein folds in plant peroxidases and yeast peroxidase and, therefore, a common evolutionary origin. The following tests support this thesis: (a) predicted helices in the plant peroxidases follow the complex pattern observed in the crystal structure of cytochrome c peroxidase; (b) their hydropathic profiles are similar and agree with observed buried and exposed peptide chain in cytochrome c peroxidase ; (c) half-cystines which are distant in the amino acid sequence of plant peroxidases become spatial neighbours when fitted into the cytochrome c peroxidase model; (d) the two-domain structure proposed from limited proteolysis of apoperoxidase HRP C is observed in the crystal structure of cytochrome c peroxidase.The similarities and differences of the plant and yeast peroxidases and the reactive side chains of a plant peroxidase active site are described. The characteristics of Ca2+-binding sequences, derived from several superfamilies, are applied to predict the Ca2 +-binding sequences in plant peroxidases.Plant peroxidases, their derivatives and catalytic intermediates have been the subject of a vast number of kinetic and spectroscopic studies. Such studies require a detailed spatial model for full interpretation. X-Ray crystallographic analysis of a plant peroxidase, however, has so far been unsuccessful, but the primary structures of horseradish peroxidase HRP C 11, 21, turnip peroxidase TP 7 [3, 41, and of the heme-linked sequences of turnip peroxidase TP 1, TP 2 and TP 3 [5] are known. This paper explores the available amino acid sequences of plant peroxidases to predict and describe molecular and structural characteristics of plant peroxidases.Recent comparison of structural and functional properties of plant peroxidases and the known hemoprotein superfamilies pointed to cytochrome c peroxidase from yeast as a possible analog. As part of the present paper, we support the thesis that plant peroxidases and cytochrome c peroxidase of yeast are structural homologues, although the reductant of cytochrome c peroxidase is a macromolecule, whereas it is a small molecule in the case of plant peroxidases. A crude model of plant peroxidases based on the recent crystal structure of cytochrome c peroxidase solved by T. Poulos et al. [6] is proposed and discussed. It is argued that the kinetic and spectral data on plant peroxidases may now confidently be interpreted in molecular terms based on the active site geometry of cytochrome c peroxidase and t...

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Isolation and Characterization of Five Neutral Isoenzymes of Horseradish Peroxidase1

Cited by 111 publications

References 0 publications

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Determination of mitochondrial reactive oxygen species: methodological aspects

Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase

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