1.8.7.1: assimilatory sulfite reductase (ferredoxin)
This is an abbreviated version!
For detailed information about assimilatory sulfite reductase (ferredoxin), go to the full flat file.
Word Map on EC 1.8.7.1
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1.8.7.1
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nitrite
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maize
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4.2.99.8
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o-acetyl-l-serine
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2.7.7.4
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sulfhydrylase
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cyanidioschyzon
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sulfurylase
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sulphite
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5'-phosphosulfate
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merolae
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viologen
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medicine
- 1.8.7.1
- nitrite
- maize
-
4.2.99.8
- o-acetyl-l-serine
-
2.7.7.4
-
sulfhydrylase
-
cyanidioschyzon
-
sulfurylase
- sulphite
- 5'-phosphosulfate
- merolae
- viologen
- medicine
Reaction
Synonyms
CMG021C, CmSiRB, coenzyme F420-dependent sulfite reductase, CYME_CMG021C, CYME_CMJ117C, DCP68, desulphoviridin, dissimilatory sulfite reductase, dSiR, EC 1.8.99.1, Fd-SiR, FdSiR, ferredoxin and sulfite reductase, ferredoxin sulfite reductase, ferredoxin-dependent sulfite reductase, ferredoxin-sulfite reductase, ferredoxin:sulfite oxidoreductase, ferredoxin:sulfite reductase, Fsr, NirA, PsSiR, SIR, SiRA, SirB, siroheme- and [Fe4-S4]-dependent NirA, sulfite reductase, sulfite reductase B, ZmSiR
ECTree
1.8.7.1 assimilatory sulfite reductase (ferredoxin)Advanced search results
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results (Engineering
Engineering on EC 1.8.7.1 - assimilatory sulfite reductase (ferredoxin)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G212S/L213T/Y214L/S217C/C220I/S221N
mutations mimic partially isoform SiRA
S217C
mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
G212S/L213T/Y214L/S217C/C220I/S221N
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mutations mimic partially isoform SiRA
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S217C
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mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
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C161A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
C161S
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69F
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
C161A
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catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
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C161S
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catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
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Y69A
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catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
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Y69F
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catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
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C491G
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
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
C491G
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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
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C491G
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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
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