The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.

@article{Eschenbrenner1995TheFR,
  title={The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.},
  author={Martin Eschenbrenner and Jacques Cov{\'e}s and Marc Fontecave},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 35},
  pages={20550-5}
}
Sulfite reductase (SiR) from Escherichia coli has a alpha 8 beta 4 subunit structure, where alpha 8 is a flavoprotein (SiR-FP) containing both FAD and FMN as prosthetic groups. It also exhibits a NADPH:flavin oxidoreductase activity with exogenous riboflavin, FMN, and FAD serving as substrates. The flavin reductase activity may function during activation of ribonucleotide reductase or during ferrisiderophore reduction. A plasmid containing cysJ gene, coding for the alpha subunit, overexpresses… CONTINUE READING

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While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
Sulfite reductase ( SiR ) from Escherichia coli has a alpha 8 beta 4 subunit structure , where alpha 8 is a flavoprotein ( SiR - FP ) containing both FAD and FMN as prosthetic groups .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
Sulfite reductase ( SiR ) from Escherichia coli has a alpha 8 beta 4 subunit structure , where alpha 8 is a flavoprotein ( SiR - FP ) containing both FAD and FMN as prosthetic groups .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
FlavinsNo subtypeNADP
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
NADPNo subtypeFlavins
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
It also exhibits a NADPH : flavin oxidoreductase activity with exogenous riboflavin , FMN , and FAD serving as substrates .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
While the FAD cofactor mediates the electron transfer between NADPH and free flavins , the FMN cofactor is not essential since a FMN - depleted SiR - FP retains a large proportion of activity .
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