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 ◽  
...  

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.

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 ◽  
...  

2020 ◽  
pp. 124336
Author(s):  
Saud Alamri ◽  
Manzer H. Siddiqui ◽  
Bishwajit Kumar Kushwaha ◽  
Vijay Pratap Singh ◽  
Hayssam M. Ali

1996 ◽  
Vol 313 (3) ◽  
pp. 841-847 ◽  
Author(s):  
Irina G. GAZARYAN ◽  
L. Mark LAGRIMINI ◽  
Gillian A. ASHBY ◽  
Roger N. F. THORNELEY

Indole-3-acetic acid (IAA) is a powerful plant growth regulator. The oxidative decarboxylation of IAA by plant peroxidases is thought to be a major degradation reaction involved in controlling the in vivo level of IAA. Horseradish peroxidase isoenzyme C and an anionic tobacco peroxidase isolated from transgenic Nicotiana sylvestris have been used in experiments in vitro designed to determine the mechanism of IAA oxidation. In particular, the initial reduction of ferric to ferrous enzyme, a key step in previously proposed mechanisms, has been investigated by rapid-scan stopped-flow spectrophotometry under strictly anaerobic conditions and at defined oxygen concentrations. The data provide the first evidence for a ternary complex comprising peroxidase, IAA and oxygen that is kinetically competent both at the initiation stage and during the catalytic cycle of IAA oxidation. A general scheme describing the oxidative cycles of both anionic and cationic peroxidases is proposed that includes native ferric enzyme and compound II as kinetically competent intermediates. For anionic peroxidases, addition of hydrogen peroxide switches on the oxidative cycle thereby promoting IAA oxidation. 2-Methyl-IAA is not a substrate of the oxidase reaction, suggesting a specific interaction between plant peroxidases and IAA.


2010 ◽  
Vol 62 (1) ◽  
pp. 59-64 ◽  
Author(s):  
L’ubica Halušková ◽  
Katarína Valentovičová ◽  
Jana Huttová ◽  
Igor Mistrík ◽  
Ladislav Tamás

1979 ◽  
Vol 57 (9) ◽  
pp. 1078-1082
Author(s):  
Annette Chappet ◽  
Martine Deschamps-Mudry ◽  
Dominique Job

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.


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