Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins
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Updated: Aug 9, 2026

Detection of Histone Modifications in Plant Leaves
Published on: September 23, 2011
P A Savitsky1, A M Rojkova, V I Tishkov
1Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia.
Abstract:
Application of computer methods allowed us to demonstrate that plant peroxidases and auxin-binding proteins contain structurally similar fragments. The mapping of the fragments was done using a model structure of horseradish peroxidase. Five of six structurally similar fragments belong to the distal domain and form a subdomain in plant peroxidases that includes the distal heme-coordinating sequence, LHFHDC (amino acid residues 39-44 in horseradish peroxidase). The existence of a substrate-binding site for indole-3-acetic acid in the distal subdomain comprising helices A (whole), B (middle), C (beginning), and D (whole) and the loop between helices D and D' is discussed.
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