title: Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B.
abstract: To investigate the flavin utilization by dibenzothiophene monooxygenase (DszC), DszC of a desulfurizing bacterium Mycobacterium goodii X7B was purified from the recombinant Escherichia coli. It was shown to be able to utilize either FMNH(2) or FADH(2) when coupled with a flavin reductase that reduces either FMN or FAD. Sequence analysis indicated that DszC was similar to the C(2) component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH(2) and FMNH(2) as substrates. Both flavins at high concentrations could inhibit the activity of DszC due to autocatalytic oxidation of reduced flavins. The results suggest that DszC should be reclassified as an FMNH(2) and FADH(2) both-utilizing monooxygenase component and the flavins should be controlled at properly reduced levels to obtain optimal biodesulfurization results.
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
authors.forename: Jingchen
authors.initials: J
authors.lastname: Li
authors.forename: Jinhui
authors.initials: J
authors.lastname: Feng
authors.forename: Qian
authors.initials: Q
authors.lastname: Li
authors.forename: Cuiqing
authors.initials: C
authors.lastname: Ma
authors.forename: Bo
authors.initials: B
authors.lastname: Yu
authors.forename: Chao
authors.initials: C
authors.lastname: Gao
authors.forename: Geng
authors.initials: G
authors.lastname: Wu
authors.forename: Ping
authors.initials: P
authors.lastname: Xu
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D055162:Biocatalysis; D001673:Biodegradation, Environmental; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005486:Flavin Mononucleotide / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000031:analogs & derivatives* / Q000378:metabolism; D008969:Molecular Sequence Data; D009161:Mycobacterium / Q000201:enzymology* / Q000235:genetics; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010802:Phylogeny; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D005182:Flavin-Adenine Dinucleotide; C058805:1,5-dihydro-FAD; D005486:Flavin Mononucleotide; D010088:Oxidoreductases; C090100:dibenzothiophene monooxygenase