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Literature summary for 1.8.5.4 extracted from

  • Lencina, A.M.; Gennis, R.B.; Schurig-Briccio, L.A.
    The oligomeric state of the Caldivirga maquilingensis type III sulfide quinone oxidoreductase is required for membrane binding (2020), Biochim. Biophys. Acta, 1861, 148132 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.5.4

Cloned(Commentary)

Cloned (Comment) Organism
gene sqr, recombinant expression of His- or FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain C43(DE3) Caldivirga maquilingensis

Protein Variants

Protein Variants Comment Organism
additional information construction of soluble mutant variants, unable to bind to the membrane, lacking either four hydrophobic residues from the last C-terminal helix (quadruple-mutant or YL), the complete last C-terminal helix (truncated 1 or T1) or the last two C-terminal helices (truncated 2 or T2). Localization study of tagged wild-type and mutant enzymes and enzyme fragments in Escherichia coli cells, overview Caldivirga maquilingensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Caldivirga maquilingensis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane CmSQR oligomerization is necessary for membrane binding, analysis of the binding of recombiant hetero-oligomers of differentially tagged CmSQR mutant variants Caldivirga maquilingensis 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83000 89000 recombinant dimeric enzyme, native PAGE Caldivirga maquilingensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
n H2S + n quinone Caldivirga maquilingensis
-
 polysulfide + n quinol
-
 ?
n H2S + n quinone Caldivirga maquilingensis IC-167
-
 polysulfide + n quinol
-
 ?

Organism

Organism UniProt Comment Textmining
Caldivirga maquilingensis
-
-
-
Caldivirga maquilingensis IC-167
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain C43(DE3) by nickel affinity chromatography, dialysis, ultracentrifugation at 230000 x g, followed by solubilization with dodecyl-beta-D-maltoside and another step of nickel affinity chromatography Caldivirga maquilingensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information quinone binding site structure analysis and binding mechanism by CmSQR, overview Caldivirga maquilingensis ?
-
-
additional information quinone binding site structure analysis and binding mechanism by CmSQR, overview Caldivirga maquilingensis IC-167 ?
-
-
n H2S + n quinone
-
 Caldivirga maquilingensis polysulfide + n quinol
-
 ?
n H2S + n quinone
-
 Caldivirga maquilingensis IC-167 polysulfide + n quinol
-
 ?
n S2- + n decylubiquinone Na2S Caldivirga maquilingensis polysulfide + n decylubiquinol
-
 ?
n S2- + n decylubiquinone Na2S Caldivirga maquilingensis IC-167 polysulfide + n decylubiquinol
-
 ?

Subunits

Subunits Comment Organism
oligomer oligomerization of CmSQR does not involve the membrane binding domain, importance of the C-terminal region for oligomerization. CmSQR oligomerization is necessary for membrane binding Caldivirga maquilingensis

Synonyms

Synonyms Comment Organism
CmSQR
-
 Caldivirga maquilingensis
III SQR
-
 Caldivirga maquilingensis
SQR
-
 Caldivirga maquilingensis
sulfide:quinone oxidoreductase
-
 Caldivirga maquilingensis
type III sulfide:quinone oxidoreductase
-
 Caldivirga maquilingensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Caldivirga maquilingensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Caldivirga maquilingensis

Cofactor

Cofactor Comment Organism Structure
FAD residues Gly12, Gly16, Ala77, and Pro44 are determined to be important for flavin binding, binding structure analysis, overview Caldivirga maquilingensis

General Information

General Information Comment Organism
evolution SQRs belong to the two-dinucleotide-binding-domains flavoprotein (tDBDF) superfamily, characterized by the presence of two Rossmann fold domains known to stabilize the adenosine moieties of dinucleotides (e.g. FAD and NADH). SQRs are typically oligomeric flavoproteins with multiple copies of a single subunit of molecular mass of about 50 kDa. SQRs are associated with the prokaryotic cytoplasmic or periplasmic membrane or the inner mitochondrial membrane Caldivirga maquilingensis
additional information residue Gly299 is only important for quinone reduction despite its proximity to bound FAD. Residues Phe337 and Phe362 are also important for quinone binding apparently by direct interaction with the quinone ring, whereas Lys359, postulated to hydrogen bond to the quinone, seems to have a more structural role. Three-dimensional homology model of Caldivirga maquilingensis SQR Caldivirga maquilingensis
physiological function sulfide:quinone oxidoreductase (SQR) is a monotopic membrane flavoprotein present in all domains of life, with multiple roles including sulfide detoxification, homeostasis and energy generation by providing electrons to respiratory or photosynthetic electron transport chains Caldivirga maquilingensis