AF245096.1

Detailed information

Microorganism
Azospirillum brasilense strain Sp245

Taxonomy
Phylum : Proteobacteria Class : Alphaproteobacteria Order : Rhodospirillales Family : Rhodospirillaceae Genus : Azospirillum

Isolation Source
nan

Enzyme Name
periplasmic nitrate reductase small diheme cytochrome c subunit

Protein Information
Pro_GenBank I.D： AAL36491.1 Length：160 aa Protein FASTA_sequence: Link

Information about Article
Reference：Steenhoudt et al., 2001 Title：Identification and characterization of a periplasmic nitrate reductase in Azospirillum brasilense Sp245 Pubmed ID：11409544.0 Pubmed link： Link Full research link： Link Abstract：The Azospirillum brasilense Sp245 napABC genes, encoding nitrate reductase activity, were isolated and sequenced. The derived protein sequences are very similar throughout the whole Nap segment to the NapABC protein sequences of Escherichia coli, Pseudomonas sp. G-179, Ralstonia eutropha, Rhodobacter sphaeroides, and Paracoccus denitrificans. Based on whole-cell nitrate reductase assays with the artificial electron donors benzyl viologen and methyl viologen, and assays with periplasmic cell-free extracts, it was concluded that the napABC-encoded enzyme activity in Azospirillum brasilense Sp245 corresponds to a periplasmic dissimilatory nitrate reductase, which was expressed under anoxic conditions and oxic conditions. A kanamycin-resistant Azospirillum brasilense Sp245 napA insertion mutant was constructed. The mutant still expressed assimilatory nitrate reductase activity, but was devoid of its periplasmic dissimilatory nitrate reductase activity.

Reference：Steenhoudt et al., 2001
Title：Identification and characterization of a periplasmic nitrate reductase in Azospirillum brasilense Sp245
Pubmed ID：11409544.0
Pubmed link： Link
Full research link： Link
Abstract：The Azospirillum brasilense Sp245 napABC genes, encoding nitrate reductase activity, were isolated and sequenced. The derived protein sequences are very similar throughout the whole Nap segment to the NapABC protein sequences of Escherichia coli, Pseudomonas sp. G-179, Ralstonia eutropha, Rhodobacter sphaeroides, and Paracoccus denitrificans. Based on whole-cell nitrate reductase assays with the artificial electron donors benzyl viologen and methyl viologen, and assays with periplasmic cell-free extracts, it was concluded that the napABC-encoded enzyme activity in Azospirillum brasilense Sp245 corresponds to a periplasmic dissimilatory nitrate reductase, which was expressed under anoxic conditions and oxic conditions. A kanamycin-resistant Azospirillum brasilense Sp245 napA insertion mutant was constructed. The mutant still expressed assimilatory nitrate reductase activity, but was devoid of its periplasmic dissimilatory nitrate reductase activity.