EC Number   |
Title |
Organism |
|---|
    1.8.1.2 | Enzymatic synthesis of gold nanoparticles using sulfite reductase purified from Escherichia coli A green eco-friendly approach |
Escherichia coli |
| 1.8.1.2 | Enzymatic synthesis of gold nanoparticles using sulfite reductase purified from Escherichia coli A green eco-friendly approach |
Escherichia coli PTCC 1330 |
| 1.8.1.2 | Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans |
Cryptococcus neoformans var. neoformans |
| 1.8.1.2 | Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans |
Cryptococcus neoformans var. neoformans ATCC MYA-565 |
| 1.8.1.2 | Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans |
Cryptococcus neoformans var. neoformans JEC21 |
| 1.8.1.2 | NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase |
Escherichia coli |
| 1.8.1.2 | Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase |
Escherichia coli |
| 1.8.1.2 | Structure-function relationships in the oligomeric NADPH-dependent assimilatory sulfite reductase |
Escherichia coli |
| 1.8.1.2 | The N-terminal domain of Escherichia coli assimilatory NADPH-sulfite reductase hemoprotein is an oligomerization domain that mediates holoenzyme assembly |
Escherichia coli |
| 1.8.1.2 | The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity |
Escherichia coli |
