Circular dichroism of turnip peroxidases

Job, Dominique; Dunford, H. Brian

doi:10.1139/o77-119

Cited by 13 publications

(4 citation statements)

References 14 publications

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“…Circular dichroism spectra of peroxidase isoenzymes of horseradish [31], turnip [32] and Japanese radish [33] are so similar that the secondary structures must be nearly identical. Concordantly, these studies estimate the content of the helix to be 35 -40% with little extended structure (Table 1).…”

Section: Secondary Structure In Plant Peroxidusesmentioning

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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Section: Secondary Structure In Plant Peroxidusesmentioning

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 latter feature was previously observed in the CD spectrum of the analogous derivative of ZPO paraperoxidase (Casella et al 1986) and appears, therefore, a common characteristic of the zocchini enzymes. The remaining portion of the CD spectrum of carbon-monoxy ferro-ZPOA, including the negative peak near 570 nm, is similar to those of the turnip (Job & Dunford 1977) and HRPA derivatives (data not shown). The far-UV CD spectrum of ZPOA (Figure 3b) is consistent with the emerging overall structural similarity of the three plant peroxidases and shows close resemblance with those of ZPO paraperoxidase (Casella et al 1986), HRP isoenzymes (Strickland et al 1968) and turnip peroxidase (Job & Dunford 1977).…”

Section: Spectral Properties Of Zpo and Hrp Anionic Isoenzymesmentioning

confidence: 64%

“…The remaining portion of the CD spectrum of carbon-monoxy ferro-ZPOA, including the negative peak near 570 nm, is similar to those of the turnip (Job & Dunford 1977) and HRPA derivatives (data not shown). The far-UV CD spectrum of ZPOA (Figure 3b) is consistent with the emerging overall structural similarity of the three plant peroxidases and shows close resemblance with those of ZPO paraperoxidase (Casella et al 1986), HRP isoenzymes (Strickland et al 1968) and turnip peroxidase (Job & Dunford 1977). An estimate of the o~-helix content of ZPOA from the ellipticity at 222 nm (Chen et al 1972), using a mean residue weight of 112 determined as before (Casella et al 1986) on the basis of the amino acid composition of HRP (Welinder 1979), gives about 30% helical content, a value in the range predicted or estimated for plant and yeast peroxidases (Welinder 1985).…”

Section: Spectral Properties Of Zpo and Hrp Anionic Isoenzymesmentioning

confidence: 64%

“…Figure 3 shows the CD spectra of native ZPOA and its reduced and carbon monoxide derivatives. These spectra bear qualitatively close relationships not only with those of HRP isoenzymes (Strickland et al 1968, Willick et al 1969 but also with those of the acidic (P1) isoenzyme of turnip peroxidase (Job & Dunford 1977). The main differences between the CD spectra of these proteins are observed in the otherwise almost featureless curves of the reduced derivatives and in the asymmetry of the Soret CD couplet of the carbonyl derivative of reduced ZPOA, exhibiting a weaker positive limb at lower energy and a stronger negative limb at higher energy.…”

Section: Spectral Properties Of Zpo and Hrp Anionic Isoenzymesmentioning

confidence: 70%

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Purification, characterization and catalytic activity of anionic zucchini peroxidase

et al. 1993

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The isolation and purification, by preparative electrofocusing, of the major anionic (ZPOA) and cationic (ZPOC) isoenzymes, collected from young zucchini squash, are reported. The Mr and sugar content are similar to those found previously for the major isoenzymes from the ripe fruits and in the range commonly observed for plant peroxidases. The amount of the two cationic enzymes was very low compared with that of anionic ZPOA. The anionic enzyme has been characterized by electronic, circular dichroism, proton NMR and electron paramagnetic resonance spectroscopy. The spectra are qualitatively similar to those of the corresponding anionic horseradish peroxidase (HRPA) derivatives, with minor differences attributable to the particular protein environment around the heme. The kinetics of the enzymatic oxidation of a series of phenols by HzO2 have been studied. ZPOA shows a parallel behavior to HRPA, but it is systematically more active than HRPA, indicating that the zucchini enzymes have a marked tendency to carry out oxidation of this type of compounds.

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Table 7.IV

Yang¹,

Wu²,

Böhm³

Landolt-Börnstein - Group VII Biophysics

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Circular dichroism of turnip peroxidases

Cited by 13 publications

References 14 publications

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

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

Purification, characterization and catalytic activity of anionic zucchini peroxidase

Table 7.IV

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