
pmid: 8389549
A soluble ferrisiderophore reductase activity of Escherichia coli was purified to homogeneity and identified as the sulfite reductase. The pure enzyme catalyzes the reduction of ferric citrate, ferriaerobactin, ferrioxamin, ferricrocin, ferrichrome and ferrifusarinin by NADPH. Free flavins, riboflavin, FMN, FAD were absolutely required, suggesting that this activity resides in the flavin reductase activity of sulfite reductase.
Chromatography, Chromatography, Ion Exchange, Substrate Specificity, Kinetics, Durapatite, Chromatography, Gel, Escherichia coli, NADH, NADPH Oxidoreductases, Oxidoreductases Acting on Sulfur Group Donors, Hydroxyapatites
Chromatography, Chromatography, Ion Exchange, Substrate Specificity, Kinetics, Durapatite, Chromatography, Gel, Escherichia coli, NADH, NADPH Oxidoreductases, Oxidoreductases Acting on Sulfur Group Donors, Hydroxyapatites
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 14 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
