EC Number   |
Protein Variants |
Reference |
|---|
    1.8.7.1 | A493G |
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity |
742806 |
| 1.8.7.1 | A503G |
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity |
742806 |
| 1.8.7.1 | Arg111Q |
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme |
742806 |
| 1.8.7.1 | Arg114Q |
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme |
742806 |
| 1.8.7.1 | Arg324Q |
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme |
742806 |
| 1.8.7.1 | C161A |
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate |
-, 674459 |
| 1.8.7.1 | C161S |
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate |
-, 674459 |
| 1.8.7.1 | C491G |
site-directed mutagenesis, the mutant shows a lower rate of H2S evolution compared to wild-type likely related to its lower cofactor content. The mutagenesis of this Cys residue to a Gly opens an exchangeable coordination site to a corner iron atom that can be chemically rescued by an external thiolate ligand. This ligand can be subsequently displaced by mass action using a dithiol molecular wire to tether two redox active proteins. Application of this technique to tethering Photosystem I to ferredoxin sulfite reductase (FdSiR). UV/Vis absorbance spectra of both FdSiRWT and the FdSiRC491G variant display characteristic peaks at 278, 392 (Soret), 585 (alpha) and 714 nm (charge transfer band), and 278, 394 (Soret), 587 (alpha) and 714 nm (charge transfer band) respectively. Both enzymes in their as-isolated forms display an EPR spectrum characteristic of an S=5/2 high spin heme. When reduced, both enzymes exhibit the signal of a low spin S=1/2 [4Fe-4S]1+ cluster. The FdSiRWT and FdSiRC491G variant both show activity using reduced methyl viologen and Synechococcus elongatus PCC 7942 ferredoxin 1 (Fd1) as electron donors. Based on these results, the FdSIRC491G variant should be a suitable candidate for wiring to Photosystem I |
-, 764195 |
| 1.8.7.1 | G212S/L213T/Y214L/S217C/C220I/S221N |
mutations mimic partially isoform SiRA |
-, 742810 |
| 1.8.7.1 | L499G |
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity |
742806 |
