scholarly journals Hydrogen Peroxide-mediated Oxidation of Indole-3-acetic Acid by Tomato Peroxidase and Molecular Oxygen

1979 ◽  
Vol 64 (2) ◽  
pp. 220-223 ◽  
Author(s):  
Demetri M. Kokkinakis ◽  
James L. Brooks
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Molecular Oxygen ◽  
Indole 3 Acetic Acid ◽  
Mediated Oxidation

scholarly journals Hydrogen peroxide is a mediator of indole-3-acetic acid/horseradish peroxidase-induced apoptosis

FEBS Letters ◽  
2006 ◽  
Vol 580 (5) ◽  
pp. 1439-1446 ◽  
Author(s):  
Dong-Seok Kim ◽  
Sang-Eun Jeon ◽  
Yun-Mi Jeong ◽  
So-Young Kim ◽  
Sun-Bang Kwon ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Horseradish Peroxidase ◽  
Induced Apoptosis ◽  
Indole 3 Acetic Acid

Mitigation of arsenate toxicity by indole-3-acetic acid in brinjal roots: Plausible association with endogenous hydrogen peroxide

2020 ◽  
pp. 124336
Author(s):  
Saud Alamri ◽  
Manzer H. Siddiqui ◽  
Bishwajit Kumar Kushwaha ◽  
Vijay Pratap Singh ◽  
Hayssam M. Ali
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Indole 3 Acetic Acid

Elevated indole-3-acetic acid peroxidase activity is involved in the cadmium-induced hydrogen peroxide production in barley root tip

2010 ◽  
Vol 62 (1) ◽  
pp. 59-64 ◽  
Author(s):  
L’ubica Halušková ◽  
Katarína Valentovičová ◽  
Jana Huttová ◽  
Igor Mistrík ◽  
Ladislav Tamás
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Peroxidase Activity ◽  
Barley Root ◽  
Root Tip ◽  
Hydrogen Peroxide Production ◽  
Indole 3 Acetic Acid ◽  
Barley Root Tip

Oxydation peroxydative de l'acide indolyl-1 acétique par une peroxydase de Raifort. Influence du pH

1979 ◽  
Vol 57 (9) ◽  
pp. 1078-1082
Author(s):  
Annette Chappet ◽  
Martine Deschamps-Mudry ◽  
Dominique Job
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Equilibrium Constant ◽  
Indole 3 Acetic Acid ◽  
Medium Acidity

Contrary to indole-3-acetic acid, indole-1-acetic acid (I1AA) may be destroyed by horseradish isoperoxydase ‘c’ (HRPc) only in the presence of hydrogen peroxide. This peroxidative reaction depends on the enzyme and H2O2 concentrations and on the medium acidity. By calculation of the binding equilibrium constant of the HRPc–I1AA complex for different pH, it appears that enzyme affinity for this substrate is higher for the more acidic tested pH.

scholarly journals Hydrogen Peroxide in the Enzymic Oxidation of Heteroauxin

1951 ◽  
Vol 4 (3) ◽  
pp. 293 ◽  
Author(s):  
PL Goldacre
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Enzymic Oxidation ◽  
Low Concentrations ◽  
Colloidal Platinum ◽  
Indole 3 Acetic Acid

A hydrogen peroxide-peroxidase system is essential to the enzymic oxidation of indole-3-acetic acid. Catalase and colloidal platinum inhibited strongly such oxidation, and extremely low concentrations of guaiacol competed with the LA.A. for the LA.A. oxidase.

The acute effect of copper on the levels of indole-3-acetic acid and lignin in peanut roots

2001 ◽  
Vol 28 (4) ◽  
pp. 329 ◽  
Author(s):  
Tsai-Chi Li ◽  
Teng-Yung Feng ◽  
Wen-Shaw Chen ◽  
Zin-Huang Liu
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Root Growth ◽  
Arachis Hypogaea ◽  
Lignin Content ◽  
Acute Effect ◽  
Significant Inhibition ◽  
Arachis Hypogaea L ◽  
Effect Of Copper ◽  
Indole 3 Acetic Acid

Cu-treated peanut (Arachis hypogaea L.) seedlings showeda significant inhibition in peanut root growth, and a decrease in endogenousindole-3-acetic acid (IAA) content. The decline of IAA content in Cu-treatedtissue was accompanied by an increase in the activity of cationic peroxidase(POD) isozyme P8.5, which was correlated with an increase in cationic PODtranscripts. Cu might suppress the growth of peanut roots by inducing thesynthesis of the cationic POD isozyme that degrades endogenous IAA. Theincrease in the activity of anionic POD isozyme P3.5 was correlated with therise in lignin content in Cu-treated roots. We suggest that the increase inanionic POD isozyme P3.5 induced by Cu might be responsible for ligninsynthesis in peanut roots, and may also remove excess hydrogen peroxide causedby Cu, thus playing a detoxifying role during Cu treatment.

scholarly journals Oxidation of indole-3-acetic acid by dioxygen catalysed by plant peroxidases: specificity for the enzyme structure

1999 ◽  
Vol 340 (3) ◽  
pp. 579-583 ◽  
Author(s):  
Pavel A. SAVITSKY ◽  
Irina G. GAZARYAN ◽  
Vladimir I. TISHKOV ◽  
L. Mark LAGRIMINI ◽  
Tautgirdas RUZGAS ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Binding Proteins ◽  
Amino Acid Sequences ◽  
Auxin Binding ◽  
Plant Peroxidases ◽  
Oxidation With Molecular Oxygen ◽  
Auxin Binding Proteins ◽  
First Time ◽  
Indole 3 Acetic Acid

Indole-3-acetic acid (IAA) can be oxidized via two mechanisms: a conventional hydrogen-peroxide-dependent pathway, and one that is hydrogen-peroxide-independent and requires oxygen. It has been shown here for the first time that only plant peroxidases are able to catalyse the reaction of IAA oxidation with molecular oxygen. Cytochrome c peroxidase (CcP), fungal peroxidases (manganese-dependent peroxidase, lignin peroxidase and Arthromyces ramosus peroxidase) and microperoxidase were essentially inactive towards IAA in the absence of added H2O2. An analysis of amino acid sequences allowed five structurally similar fragments to be identified in auxin-binding proteins and plant peroxidases. The corresponding fragments in CcP and fungal peroxidases showed no similarity with auxin-binding proteins. Five structurally similar fragments form a subdomain including the catalytic centre and two residues highly conserved among ‘classical’ plant peroxidases only, namely His-40 and Trp-117. The subdomain identified above with the two residues might be responsible for the oxidation of the physiological substrate of classical plant peroxidases, IAA.

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