Oxidation of Indole-3-acetic Acid by Dioxygen Catalysed by Plant Peroxidases: Specificity for the Enzyme Structure

Overview

Journal Biochem J

Specialty Biochemistry

Date 1999 Jun 9

PMID 10359640

Citations 20

Authors

P A Savitsky

I G Gazaryan

V I Tishkov

L M Lagrimini

T Ruzgas

L Gorton

Affiliations

Soon will be listed here.

Abstract

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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References

Petersen J, Kadziola A, Larsen S . Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution. FEBS Lett. 1994; 339(3):291-6. DOI: 10.1016/0014-5793(94)80433-8. View

Kunishima N, Fukuyama K, Matsubara H, Hatanaka H, Shibano Y, Amachi T . Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases. J Mol Biol. 1994; 235(1):331-44. DOI: 10.1016/s0022-2836(05)80037-3. View

Gazarian I, Lagrimini L . Anaerobic stopped-flow studies of indole-3-acetic acid oxidation by dioxygen catalysed by horseradish C and anionic tobacco peroxidase at neutral pH: catalase effect. Biophys Chem. 2006; 72(3):231-7. DOI: 10.1016/s0301-4622(98)00098-2. View

Picot D, Loll P, Garavito R . The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature. 1994; 367(6460):243-9. DOI: 10.1038/367243a0. View

Klotz K, Lagrimini L . Phytohormone control of the tobacco anionic peroxidase promoter. Plant Mol Biol. 1996; 31(3):565-73. DOI: 10.1007/BF00042229. View

Schuller D, Ban N, Huystee R, McPherson A, Poulos T . The crystal structure of peanut peroxidase. Structure. 1996; 4(3):311-21. DOI: 10.1016/s0969-2126(96)00035-4. View

Altschul S, Gish W, Miller W, Myers E, Lipman D . Basic local alignment search tool. J Mol Biol. 1990; 215(3):403-10. DOI: 10.1016/S0022-2836(05)80360-2. View

Finzel B, Poulos T, KRAUT J . Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. J Biol Chem. 1984; 259(21):13027-36. View

Krylov S, Brian Dunford H . Evidence for a free radical chain mechanism in the reaction between peroxidase and indole-3-acetic acid at neutral pH. Biophys Chem. 1996; 58(3):325-34. DOI: 10.1016/0301-4622(95)00102-6. View

10.

Gajhede M, Schuller D, Henriksen A, Smith A, Poulos T . Crystal structure of horseradish peroxidase C at 2.15 A resolution. Nat Struct Biol. 1997; 4(12):1032-8. DOI: 10.1038/nsb1297-1032. View

11.

Gazaryan I, Lagrimini L, Ashby G, Thorneley R . Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases. Biochem J. 1996; 313 ( Pt 3):841-7. PMC: 1216987. DOI: 10.1042/bj3130841. View

12.

Lambeir A, Markey C, Dunford H, Marnett L . Spectral properties of the higher oxidation states of prostaglandin H synthase. J Biol Chem. 1985; 260(28):14894-6. View

13.

Gazarian I, Lagrimini L, Mellon F, Naldrett M, Ashby G, Thorneley R . Identification of skatolyl hydroperoxide and its role in the peroxidase-catalysed oxidation of indol-3-yl acetic acid. Biochem J. 1998; 333 ( Pt 1):223-32. PMC: 1219576. DOI: 10.1042/bj3330223. View

14.

Ushijima Y, Nakano M, Takyu C, Inaba H . Chemiluminescence in L-tyrosine-H2O2-horseradish peroxidase system: possible formation of tyrosine cation radical. Biochem Biophys Res Commun. 1985; 128(2):936-41. DOI: 10.1016/0006-291x(85)90136-6. View

15.

Gazaryan I, Lagrimini L . Purification and unusual kinetic properties of a tobacco anionic peroxidase. Phytochemistry. 1996; 41(4):1029-34. DOI: 10.1016/0031-9422(95)00779-2. View

16.

Sundaramoorthy M, Kishi K, Gold M, Poulos T . The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem. 1994; 269(52):32759-67. View

17.

Poulos T, Edwards S, Wariishi H, Gold M . Crystallographic refinement of lignin peroxidase at 2 A. J Biol Chem. 1993; 268(6):4429-40. DOI: 10.2210/pdb1lga/pdb. View

18.

HINMAN R, LANG J . PEROXIDASE-CATALYZED OXIDATION OF INDOLE-3-ACETIC ACID. Biochemistry. 1965; 4:144-58. DOI: 10.1021/bi00877a023. View