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Title 

Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase

Authors 

Myung Hee KimYoonJeong KimH J ParkJong Suk LeeSu Nam GwakWoo Hyuk JungSeung Goo LeeDoo Il KimY C LeeTae Kwang Oh

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2008

Citation 

Journal of Biological Chemistry, vol. 283, no. 46, pp. 31981-31990

Keywords 

bioremediationdyesvat dyesstructural insightsstructural similaritiestriphenylmethane dyestriphenylmethane reductasesnicotinamide adenine dinucleotide phosphateoxidoreductasetriphenylmethane derivative

Abstract 

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-A 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

Link 

http://dx.doi.org/10.1074/jbc.M804092200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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