| Literature DB >> 17846764 |
Guangfei Liu1, Jiti Zhou, Hong Lv, Xuemin Xiang, Jing Wang, Mi Zhou, Yuanyuan Qv.
Abstract
Previously reported azoreductase (AZR) from Rhodobacter sphaeroides AS1.1737 was shown to be a flavodoxin possessing nitroreductase and flavin mononucleotide (FMN) reductase activities. The structure model of AZR constructed with SWISS-MODEL displayed a flavodoxin-like fold with a three-layer alpha/beta/alpha structure. With nitrofurazone as substrate, the optimal pH value and temperature were 7.0 and 50 degrees C, respectively. AZR could reduce a number of nitroaromatic compounds including 2,4-dinitrotoluene, 2,6-dinitrotoluene, 3,5-dinitroaniline, and 2,4,6-trinitrotoluene (TNT). TNT resulted to be the most efficient nitro substrate and was reduced to hydroxylamino-dinitrotoluene. Both NADH and NADPH could serve as electron donors of AZR, where the latter was preferred. Externally added FMN was also reduced by AZR via ping-pong mechanism and was a competitive inhibitor of NADPH, methyl red, and nitrofurazone. AZR with broad substrate specificity is a member of a new nitro/FMN reductase family demonstrating potential application in bioremediation.Entities:
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Year: 2007 PMID: 17846764 DOI: 10.1007/s00253-007-1087-5
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN: 0175-7598 Impact factor: 4.813