IRON REDUCTASES FROM PSEUDOMONAS-AERUGINOSA
IRON REDUCTASES FROM PSEUDOMONAS-AERUGINOSA
复制标题
DOI:
10.1128/jb.141.1.199-204.1980
复制
发表时间:
1980-01-01
影响因子:
3.2
通讯作者:
COX, CD
中科院分区:
文献类型:
--
作者:
COX, CD
Cell-free extracts of P. aeruginosa contain enzyme activities which reduce Fe(III) to Fe(II) when Fe is provided in certain chelates, but not when the Fe is uncomplexed. Iron reductase activities for 2 substrates, ferripyochelin and ferric citrate, appear to be separate enzymes because of differences in heat stabilities, in locations in fractions of cell-free extracts, in reductant specificity and in apparent sizes during gel filtration chromatography. Ferric citrate iron reductase is an extremely labile activity found in the cytoplasmic fraction and ferripyochelin iron reductase is a more stable activity found in the periplasmic as well as cytoplasmic fraction of extracts. A small amount of activity detectable in the membrane fraction seemed to be loosely associated with the membranes. Although both enzymes have highest activity with NADH, reduced glutathione also worked with ferripyochelin iron reductase. O2 caused an irreversible loss of a percentage of the ferripyochelin iron reductase following sparge of reaction mixtures, whereas the reductase for ferric citrate was not appreciably affected by O2.