Structural Insight into Bioremediation of Triphenylmethane Dyes by Citrobacter sp. Triphenylmethane Reductase

Triphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes th...

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Bibliographic Details
Published in:The Journal of biological chemistry 2008-11, Vol.283 (46), p.31981-31990
Main Authors: Kim, Myung Hee, Kim, Yoonjeong, Park, Hyo-Jung, Lee, Jong Suk, Kwak, Su-Nam, Jung, Woo-Hyuk, Lee, Seung-Goo, Kim, Dooil, Lee, Young-Choon, Oh, Tae-Kwang
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biodegradation, Environmental
Catalytic Domain
Citrobacter - enzymology
Citrobacter - genetics
Coloring Agents - chemistry
Coloring Agents - metabolism
Crystallography, X-Ray
Kinetics
Models, Molecular
Molecular Sequence Data
NADP - chemistry
NADP - metabolism
Oxidoreductases - chemistry
Oxidoreductases - genetics
Oxidoreductases - metabolism
Protein Binding
Protein Structure, Quaternary
Protein Structure, Tertiary
Rosaniline Dyes - chemistry
Rosaniline Dyes - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Trityl Compounds - chemistry
Trityl Compounds - metabolism
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Summary:Triphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes the reduction of triphenylmethane dyes. Information from the primary amino acid sequence suggests that TMR is a dinucleotide-binding motif-containing enzyme; however, no other functional clues can be derived from sequence analysis. We present the crystal structure of TMR in complex with NADP+ at 2.0-Å resolution. Despite limited sequence similarity, the enzyme shows remarkable structural similarity to short-chain dehydrogenase/reductase (SDR) family proteins. Functional assignments revealed that TMR has features of both classic and extended SDR family members and does not contain a conserved active site. Thus, it constitutes a novel class of SDR family proteins. On the basis of simulated molecular docking using the substrate malachite green and the TMR/NADP+ crystal structure, together with site-directed mutagenesis, we have elucidated a potential molecular mechanism for triphenylmethane dye reduction.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M804092200