Fenton-like Inactivation of Tobacco Peroxidase Electrocatalysis at Negative Potentials

ACS Catalysis ◽  
2016 ◽  
Vol 6 (11) ◽  
pp. 7452-7457 ◽  
Author(s):  
José Luis Olloqui-Sariego ◽  
Galina S. Zakharova ◽  
Andrey A. Poloznikov ◽  
Juan José Calvente ◽  
Dmitry M. Hushpulian ◽  
...  
Keyword(s):  
Tobacco Peroxidase

Glutamic acid-141: a heme ‘bodyguard’ in anionic tobacco peroxidase

2007 ◽  
Vol 388 (4) ◽  
pp. 373-380 ◽  
Author(s):  
Dmitri M. Hushpulian ◽  
Andrew A. Poloznikov ◽  
Pavel A. Savitski ◽  
Alexandra M. Rozhkova ◽  
Tatyana A. Chubar ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Active Center ◽  
Structural Alignment ◽  
Wild Type ◽  
E Coli ◽  
Anionic Peroxidase ◽  
Glutamic Acid Residue ◽  
Plant Peroxidases ◽  
Tobacco Peroxidase

Abstract The role of the conserved glutamic acid residue in anionic plant peroxidases with regard to substrate specificity and stability was examined. A Glu141Phe substitution was generated in tobacco anionic peroxidase (TOP) to mimic neutral plant peroxidases such as horseradish peroxidase C (HRP C). The newly constructed enzyme was compared to wild-type recombinant TOP and HRP C expressed in E. coli. The Glu141Phe substitution supports heme entrapment during the refolding procedure and increases the reactivation yield to 30% compared to 7% for wild-type TOP. The mutation reduces the activity towards ABTS, o-phenylenediamine, guaiacol and ferrocyanide to 50% of the wild-type activity. No changes are observed with respect to activity for the lignin precursor substrates, coumaric and ferulic acid. The Glu141Phe mutation destabilizes the enzyme upon storage and against radical inactivation, mimicking inactivation in the reaction course. Structural alignment shows that Glu141 in TOP is likely to be hydrogen-bonded to Gln149, similar to the Glu143-Lys151 bond in Arabidopsis A2 peroxidase. Supposedly, the Glu141-Gln149 bond provides TOP with two different modes of stabilization: (1) it prevents heme dissociation, i.e., it ‘guards’ heme inside the active center; and (2) it constitutes a shield to protect the active center from solvent-derived radicals.

Biocatalytic properties of recombinant tobacco peroxidase in chemiluminescent reaction

2007 ◽  
Vol 25 (2-4) ◽  
pp. 163-170 ◽  
Author(s):  
Dmitri M. Hushpulian ◽  
Andrew A. Poloznikov ◽  
Pavel A. Savitski ◽  
Alexandra M. Rozhkova ◽  
Tatyana A. Chubar ◽  
...  
Keyword(s):  
Chemiluminescent Reaction ◽  
Tobacco Peroxidase

scholarly journals Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

2005 ◽  
Vol 60 (6) ◽  
pp. 558-566 ◽  
Author(s):  
I. G. Gazaryan ◽  
L. Gorton ◽  
T. Ruzgas ◽  
E. Csoregi ◽  
W. Schuhmann ◽  
...  
Keyword(s):  
Amperometric Biosensors ◽  
Tobacco Peroxidase

scholarly journals Identification of skatolyl hydroperoxide and its role in the peroxidase-catalysed oxidation of indol-3-yl acetic acid

1998 ◽  
Vol 333 (1) ◽  
pp. 223-232 ◽  
Author(s):  
Irina G. GAZARIAN ◽  
L. Mark LAGRIMINI ◽  
Fred A. MELLON ◽  
Michael J. NALDRETT ◽  
Gillian A. ASHBY ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Plant Hormone ◽  
General Scheme ◽  
In Planta ◽  
Peroxidase Isoenzyme ◽  
Catalysed Reaction ◽  
Catalysed Oxidation ◽  
Hydroperoxide Formation ◽  
Tobacco Peroxidase

Indol-3-yl acetic acid (IAA, auxin) is a plant hormone whose degradation is a key determinant of plant growth and development. The first evidence for skatolyl hydroperoxide formation during the plant peroxidase-catalysed degradation of IAA has been obtained by electrospray MS. Skatolyl hydroperoxide degrades predominantly non-enzymically to oxindol-3-yl carbinol but in part enzymically into indol-3-yl methanol via a peroxidase cycle in which IAA acts as an electron donor. Skatolyl hydroperoxide is degradable by catalase. Horseradish peroxidase isoenzyme C (HRP-C) and anionic tobacco peroxidase (TOP) exhibit differences in their mechanisms of reaction. The insensitivity of the HRP-C-catalysed reaction to catalase is ascribed to the formation of HRP-C Compound III at the initiation step and its subsequent role in radical propagation. This is in contrast with the TOP-catalysed process in which skatolyl hydroperoxide has a key role. Indol-3-yl aldehyde is produced not via the peroxidase cycle but by catalysis involving ferrous peroxidase. Because indol-3-yl aldehyde is one of the main IAA-derived products identified in planta, we conclude that ferrous peroxidases participate in IAA catalytic transformations in vivo. A general scheme for peroxidase-catalysed IAA oxidation is presented.

scholarly journals An HR-Induced Tobacco Peroxidase Gene Is Responsive to Spermine, but Not to Salicylate, Methyl Jasmonate, and Ethephon

2000 ◽  
Vol 13 (2) ◽  
pp. 210-216 ◽  
Author(s):  
Susumu Hiraga ◽  
Hiroyuki Ito ◽  
Hiromoto Yamakawa ◽  
Norihiro Ohtsubo ◽  
Shigemi Seo ◽  
...  
Keyword(s):  
Gene Expression ◽  
Methyl Jasmonate ◽  
Hypersensitive Reaction ◽  
N Gene ◽  
Pr Genes ◽  
Tobacco Plants ◽  
Induced Expression ◽  
Peroxidase Gene ◽  
Induction Kinetics ◽  
Tobacco Peroxidase

In Tobacco mosaic virus (TMV)-infected tobacco plants carrying the N resistance gene, a hypersensitive reaction or response (HR) occurs to enclose the virus in the infected tissue. Although a contribution of peroxidases to the resistance has been proposed, no evidence has been presented that tobacco peroxidase genes respond to HR. Here, we describe the HR-induced expression of a tobacco peroxidase gene (tpoxC1) whose induction kinetics were slightly different from those of acidic and basic tobacco pathogenesis-related (PR) protein genes. Interestingly, tpoxC1 was insensitive to the inducers of PR genes such as salicylic acid, methyl jasmonate, and ethephon. Spermine activated tpoxC1 gene expression at a low level and both acidic and basic PR gene expression at a considerably higher level. These results indicate that the induced expression of tpoxC1 is regulated differently from that of classical tobacco PR genes in the N gene-mediated self-defense system in tobacco plants.

Direct electrochemistry of recombinant tobacco peroxidase on gold

2005 ◽  
Vol 7 (12) ◽  
pp. 1291-1297 ◽  
Author(s):  
Elena E. Ferapontova ◽  
John Castillo ◽  
Dmitri Hushpulian ◽  
Vladimir Tishkov ◽  
Tatiana Chubar ◽  
...  
Keyword(s):  
Direct Electrochemistry ◽  
Tobacco Peroxidase

Direct and Mediated Electron Transfer Catalyzed by Anionic Tobacco Peroxidase: Effect of Calcium Ions

2000 ◽  
Vol 88 (1-3) ◽  
pp. 321-334 ◽  
Author(s):  
Florentina-Daniela Munteanu ◽  
Lo Gorton ◽  
Annika Lindgren ◽  
Tautgirdas Ruzgas ◽  
Jenny Emnéus ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Calcium Ions ◽  
Mediated Electron Transfer ◽  
Tobacco Peroxidase

scholarly journals Expression of a Chimeric Tobacco Peroxidase Gene in Transgenic Tomato Plants

1992 ◽  
Vol 117 (6) ◽  
pp. 1012-1016 ◽  
Author(s):  
L. Mark Lagrimini ◽  
Jill Vaughn ◽  
John Finer ◽  
Karen Klotz ◽  
Patrick Rubaihayo
Keyword(s):  
Peroxidase Activity ◽  
Tomato Fruit ◽  
Cauliflower Mosaic Virus ◽  
Soluble Solids ◽  
Foreign Gene ◽  
Peroxidase Isoenzyme ◽  
Tomato Plants ◽  
Anionic Peroxidase ◽  
Peroxidase Gene ◽  
Tobacco Peroxidase

Tomato plants (Lycopersicon esculentum cv. OH 7814) were transformed via Agrobacterium tumefaciens with a chimeric tobacco anionic peroxidase (EC 1.11.1.7) gene joined to the cauliflower mosaic virus (CaMV) 35S promoter. Transgenic plants obtained by selection on kanamycin were found to have more than five times the total leaf peroxidase activity of control plants. Transformed tomato plants chronically wilted upon reaching sexual maturity. Two independently selected transformants were self-fertilized, and progeny were obtained that were homozygous for the foreign gene. Isoelectric focusing gels stained for peroxidase activity revealed a new tomato leaf peroxidase isoenzyme with a pI of 3.75, which is similar to that seen in Nicotiana sylvestris L. Mature tomato fruit were found to have up to 1600-fold higher peroxidase activity in transformants expressing the tobacco anionic peroxidase (TobAnPOD) than control plants. Tissue blots showed the tobacco enzyme evenly distributed throughout the tomato fruit tissue. Progeny plants possessing the tobacco peroxidase gene (now homozygous) showed stunting, and fruit size was reduced by >80%. However, fruit set was normal and the rate of ripening was not altered from control plants. Fruit from transformed plants were found to have normal pigmentation, but the soluble solids concentration was 400% higher than in control tomato fruit. This result was predicted from the peroxidase-induced water stress. Possible roles for the tobacco anionic peroxidase in growth, development, and stress resistance are discussed.

Interprotein Coupling Enhances the Electrocatalytic Efficiency of Tobacco Peroxidase Immobilized at a Graphite Electrode

2015 ◽  
Vol 87 (21) ◽  
pp. 10807-10814 ◽  
Author(s):  
José Luis Olloqui-Sariego ◽  
Galina S. Zakharova ◽  
Andrey A. Poloznikov ◽  
Juan José Calvente ◽  
Dmitry M. Hushpulian ◽  
...  
Keyword(s):  
Graphite Electrode ◽  
Tobacco Peroxidase
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