Crystal Structure of 2-nitropropane Dioxygenase Complexed with Fmn and Substrate. Identification of the Catalytic Base.
From: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea.
The Journal of biological chemistry
- Publish Date: Jul 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 27
- Pages: 18660-7
- Medium: Print
- Language: English
- Citation (JAMA): Ha Jun Yong, Min Ji Young, Lee Su Kyung, et al. Crystal Structure of 2-nitropropane Dioxygenase Complexed with Fmn and Substrate. Identification of the Catalytic Base.. J. Biol. Chem. Jul 2006;281:18660-7
Abstract
Nitroalkane compounds are widely used in chemical industry and are also produced by microorganisms and plants. Some nitroalkanes have been demonstrated to be carcinogenic, and enzymatic oxidation of nitroalkanes is of considerable interest. 2-Nitropropane dioxygenases from Neurospora crassa and Williopsis mrakii (Hansenula mrakii), members of one family of the nitroalkane-oxidizing enzymes, contain FMN and FAD, respectively. The enzymatic oxidation of nitroalkanes by 2-nitropropane dioxygenase operates by an oxidase-style catalytic mechanism, which was recently shown to involve the formation of an anionic flavin semiquinone. This represents a unique case in which an anionic flavin semiquinone has been experimentally observed in the catalytic pathway for oxidation catalyzed by a flavin-dependent enzyme. Here we report the first crystal structure of 2-nitropropane dioxygenase from Pseudomonas aeruginosa in two forms: a binary complex with FMN and a ternary complex with both FMN and 2-nitropropane. The structure identifies His(152) as the proposed catalytic base, thus providing a structural framework for a better understanding of the catalytic mechanism.
Mesh Headings (Keywords): Amino Acid Sequence, Bacterial Proteins, Binding Sites, Catalytic Domain, Dioxygenases, Flavin Mononucleotide, Histidine, Models, Molecular, Molecular Sequence Data, Neurospora crassa, Nitroparaffins, Propane, Protein Binding, Protein Conformation, Pseudomonas aeruginosa, Sequence Alignment, Substrate Specificity
Check for Full Text / PubMed Unique Identifier (PMID): 16682407
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