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Information on EC 1.8.7.1 - assimilatory sulfite reductase (ferredoxin)
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EC Tree
1.8.7.1 assimilatory sulfite reductase (ferredoxin)IUBMB Comments
An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria . Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH).
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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
3
+
3
=
+
3
+
6
Synonyms
cmsirb, zmsir, ferredoxin-dependent sulfite reductase, ferredoxin-sulfite reductase, ferredoxin sulfite reductase, pssir, dcp68, cmg021c, fdsir, ferredoxin and sulfite reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYME_CMG021C
CYME_CMJ117C
desulphoviridin
-
-
-
-
EC 1.8.99.1
-
-
formerly, part transferred
-
Fd-SiR
FdSiR
ferredoxin sulfite reductase
ferredoxin-dependent sulfite reductase
ferredoxin-sulfite reductase
ferredoxin:sulfite reductase
NirA
SIR
SiRA
SirB
siroheme- and [Fe4-S4]-dependent NirA
sulfite reductase
ferredoxin-sulfite reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin + 6 H+
extracted protein probably dual function as a major constituent of the organellar nucleoid and as the redox enzyme ferredoxin-sulfite reductase
-
hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin + 6 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
additional information
oxidation
-
-
-
-
reduction
-
-
-
-
additional information
-
sodium salts of thiosulfate and sulfate does not serve as the electron acceptor for reduced F420 oxidation by Fsr. Also, Fsr can not use NADH and NADPH for the reduction of sulfite.
additional information
-
the N-terminal half of Fsr represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
,
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SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:ferredoxin oxidoreductase
An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria [4]. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH).
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CAS REGISTRY NUMBER
COMMENTARY
37256-50-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ammonium + oxidized ferredoxin + H2O
nitrite + reduced ferredoxin + H+
-
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
hydrogen sulfide + oxidized methyl viologen + H2O
sulfite + reduced methyl viologen + H+
-
-
-
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
-
sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
-
-
?
sulfite + reduced coenzyme F420
sulfide + oxidized coenzyme F420
-
-
-
-
?
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
-
sulfur assimilation for cysteine and methionine biosynthesis
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
-
-
-
r
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
-
-
-
?
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
-
-
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
-
-
-
-
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
assimilatory sulfate reduction
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
ferredoxin can be partially replaced by benzyl viologen
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
reduced methyl viologen as electron donor also
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
ferredoxin can be partially replaced by benzyl viologen
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
reduced methyl viologen as electron donor also
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas No. 9332
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
PsSiR binds to both double-stranded and single-stranded DNA without significant sequence specificity. DNA binding does not affect the enzymatic activity of PsSiR, suggesting that ferredoxin and sulfite are accessible to SiR molecules within the nucleoids
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
reduced methyl viologen as electron donor also
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
three isoforms of ferredoxin: ferredoxin I, II and III, ferredoxin I and II in leaves, ferredoxin III in roots, ferredoxin I and III shows a comparable ability to donate electrons to enzyme
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
PsSiR binds to both double-stranded and single-stranded DNA without significant sequence specificity. DNA binding does not affect the enzymatic activity of PsSiR, suggesting that ferredoxin and sulfite are accessible to SiR molecules within the nucleoids
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
r
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
r
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
r
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
-
-
-
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
-
-
-
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
-
-
-
r
additional information
?
-
-
enzyme activites of shoot and root increase by sulfate limitation in the early stage of growth
-
-
?
additional information
?
-
-
no activity with NADPH as single electron donor
-
-
?
additional information
?
-
enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
-
-
?
additional information
?
-
enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
-
-
?
additional information
?
-
-
enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
-
-
?
additional information
?
-
enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
-
-
?
additional information
?
-
enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
-
-
?
additional information
?
-
NirA has a pronounced preference for sulfite over nitrite as substrate
-
-
?
additional information
?
-
-
NirA has a pronounced preference for sulfite over nitrite as substrate
-
-
?
additional information
?
-
NirA has a pronounced preference for sulfite over nitrite as substrate
-
-
?
additional information
?
-
-
no activity with NADPH as single electron donor
-
-
?
additional information
?
-
ferredoxin:SiR complex formation and interprotein affinity are thermodynamically adjusted by both enthalpy and entropy through electrostatic and non-electrostatic interactions. A combination of electrostatic and non-electrostatic forces stabilizes the complex with similar interfaces and modulates the binding affinity and mode
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
-
-
-
?
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
-
sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
-
-
?
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
-
sulfur assimilation for cysteine and methionine biosynthesis
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
assimilatory sulfate reduction
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas No. 9332
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
-
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Fe-S center
the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
Ferredoxin
the enzyme can use its endogenous ferredoxin as well as the ferredoxin pssm2-Fd from its parasite myovirus P-SSM2. pssm2-Fd contains sequence features of host Fds, structure of the pssm2-Fd and structure comparisons, overview. Prochlorococcus marinus ferredoxin contains [4Fe-4S] centers, the myoviral ferredoxin contains [2Fe-2S] centers
-
siroheme
-
one per enzyme subunit, in the high-spin Fe3+ state in the reduced enzyme
siroheme
-
1 mol per mol subunit, in the high-spin Fe3+ state in the reduced enzyme
additional information
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
-
additional information
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
-
additional information
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S
Fe2+
in Fe-S centers, determination of non-heme iron content of FdSiR
NaCl
at 40-70 mM NaCl in 50 mM Tris/HCl buffer, close to the physiological conditions in plant chloroplasts, delicate interprotein regulation optimizes SiR activity. At NaCl concentrations above several hundred millimolar, collision and diffusion may limit the formation of the stable electron-transfer competent complex
tungstate
tungstate
-
1 mM tungstate improves enzyme activity in Arabidopsis leaf by 29%
tungstate
-
1 mM tungstate improves enzyme activity in Arabidopsis leaf by 12%
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-acetylsuccinimide
-
inhibition of the ferredoxin-linked activity without inhibiting the methyl viologen-linked activity
N-bromosuccinimide
-
treatment leads to a loss of enzymatic activity with reduced ferredoxin and reduced methyl viologen
Phenylglyoxal
-
inhibition of the ferredoxin-linked activity and the methyl viologen-linked activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
NADPH as an additional electron donor to methyl viologen enhances enzyme activity by 1.6fold
NADPH
-
the addition of NADPH to the reaction medium increases enzyme activity by 1.6fold
NADPH
-
NADPH as an additional electron donor to methyl viologen enhances enzyme activity by 2.8fold
NADPH
-
the addition of NADPH to the reaction medium increases enzyme activity by 2.8fold
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site.