catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue

The dye-decolorizing peroxidase (DyP)-type peroxidase family is a unique heme peroxidase family. The primary and tertiary structures of this family are obviously different from those of other heme peroxidases. However, the details of the structure-function relationships of this family remain poorly...

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Bibliographic Details
Published in:The FEBS journal 2011-07, Vol.278 (13), p.2387-2394
Main Authors: Yoshida, Toru, Tsuge, Hideaki, Konno, Hiroki, Hisabori, Toru, Sugano, Yasushi
Format: Article
Language:English
Subjects:
aspartic acid
Aspartic Acid - chemistry
Aspartic Acid - metabolism
Binding Sites
Biochemistry
Catalysis
catalytic mechanism
Coloring Agents - chemistry
Coloring Agents - metabolism
Crystal structure
Crystallography, X-Ray
cyanides
DyP
DyP‐type peroxidase
Enzymes
heme
Heme - chemistry
heme iron
heme protein
hydrogen peroxide
Hydrogen Peroxide - metabolism
Molecular biology
mutants
Mutation - genetics
Oxidants - metabolism
peroxidase
Peroxidases - chemistry
Peroxidases - genetics
Peroxidases - metabolism
Protein Binding
structure-activity relationships
swing mechanism
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Summary:The dye-decolorizing peroxidase (DyP)-type peroxidase family is a unique heme peroxidase family. The primary and tertiary structures of this family are obviously different from those of other heme peroxidases. However, the details of the structure-function relationships of this family remain poorly understood. We show four high-resolution structures of DyP (EC1.11.1.19), which is representative of this family: the native DyP (1.40 Å), the D171N mutant DyP (1.42 Å), the native DyP complexed with cyanide (1.45 Å), and the D171N mutant DyP associated with cyanide (1.40 Å). These structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. Moreover, these structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron. On the basis of these results, we propose a swing mechanism in compound I formation. When DyP reacts with hydrogen peroxide, OD2 swings towards an optimal position to accept the proton from hydrogen peroxide bound to the heme iron.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2011.08161.x