Acquisition of iron by enterococci: some properties and role of assimilating ferric iron reductases.
Ferric iron reductases activities have been occurred in 91% of investigated enterococci strains. Maximum activity occurred with coenzyme NADH as the reductant and the presence of cofactor FMN was necessary. Mg(II) ions has not stimulated reductases activity. Treatment of cells with proteolytic enzymes had not effect on iron reduction. The whole cells and cell fraction-cytoplasmic membrane and cytoplasm showed Fe(III)-reducing activity. The highest specific activity was associated with cytoplasm. The activity in cytoplasmic membrane was not related to iron concentration in the growth medium. In cytoplasm the activity was stimulated after growth in low-iron medium. Ferric iron reductases of enterococci characterized the broad substrate specificity. The iron in form of ferric ammonium citrate, lactoferrin and ferrioxamine B were the best iron sources for enterococcal ferric iron reductases.
Lisiecki
Paweł
P
Department of Pharmaceutical Microbiology, Medical University, Lódź, Poland. lisiecki@toya.net.pl
Mikucki
Jerzy
J
D002458:Cell Fractionation; D019286:Endopeptidase K / Q000378:metabolism; D016983:Enterococcus / Q000201:enzymology*; D038181:FMN Reductase / Q000032:analysis / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D009243:NAD; D009249:NADP; D005486:Flavin Mononucleotide; D007501:Iron; D038181:FMN Reductase; C023903:ferric citrate iron reductase; D014357:Trypsin; D019286:Endopeptidase K