Ferrisiderophore reductase activity associated with an aromatic biosynthetic enzyme complex in Bacillus subtilis.
AUTOR(ES)
Gaines, C G
RESUMO
The cytoplasmic fractions obtained from Bacillus subtilis strains W168 and WB2802 catalyzed reductive release of iron from the ferric chelate of 2,3-dihydroxybenzoic acid (ferri-DHB), the ferrisiderophore produced by B. subtilis. Ferrisiderophore reductase activity may insert iron into metabolism. This activity required a reductant (reduced nicotinamide adenine dinucleotide phosphate was preferred), was oxygen sensitive, and was stimulated by flavin mononucleotide plus certain divalent cations. The cytoplasmic fractions also reduced 2,6-dichlorophenolindophenol; this reaction was stimulated by flavin mononucleotide plus a divalent cation. Ferri-DHB and 2,6-dichlorophenolindophenol reductase activities were copurified by phosphocellulose and diethylaminoethyl-cellulose chromatography. Nondenaturing polyacrylamide gel electrophoresis of the purified material revealed that both ferri-DHB and 2,6-dichlorophenolindophenol reductase activities were located in a protein band at Rf 0.75. The chromatographic procedures purified a reductase known to be associated with two aromatic biosynthetic enzymes, chorismate synthase and dehydroquinate synthase. Therefore, a portion of the ferrisiderophore reductase activity in B. subtilis may be catalyzed by a reductase that also is essential for aromatic biosynthesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=216236Documentos Relacionados
- Ferrisiderophore reductase activity in Bacillus megaterium.
- An enzyme common to histidine and aromatic amino acid biosynthesis in Bacillus subtilis.
- Heme Inhibition of Ferrisiderophore Reductase in Bacillus subtilis
- Ferrisiderophore reductase activity in Agrobacterium tumefaciens.
- Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis.