Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.5.1 extracted from

  • Herzog, E.; Gu, W.; Juhnke, H.D.; Haas, A.H.; Maentele, W.; Simon, J.; Helms, V.; Lancaster, C.R.
    Hydrogen-bonded networks along and bifurcation of the E-pathway in quinol:fumarate reductase (2012), Biophys. J., 103, 1305-1314.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.5.1

Protein Variants

Protein Variants Comment Organism
E180Q site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate Wolinella succinogenes
E66Q site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate Wolinella succinogenes
H44E site-diirected mutagenesis, although the H44E variant enzyme retains both heme groups, it is unable to catalyze quinol oxidation, the mutant catalyzes the electron transfer from succinate to methylene blue, with reduced activity compared to the wild-type enzyme but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate Wolinella succinogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound Helicobacter pylori 16020
-
membrane bound Wolinella succinogenes 16020
-
membrane bound Campylobacter jejuni 16020
-

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
-
-
-
Helicobacter pylori
-
-
-
Wolinella succinogenes
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,3-dimethyl-1,4-naphthoquinol + fumarate
-
 Wolinella succinogenes ?
-
 ?
succinate + methylene blue
-
 Wolinella succinogenes ?
-
 ?

Subunits

Subunits Comment Organism
oligomer homodimeric complex of heterotrimers of A, B, and C subunits Helicobacter pylori
oligomer homodimeric complex of heterotrimers of A, B, and C subunits Wolinella succinogenes
oligomer homodimeric complex of heterotrimers of A, B, and C subunits Campylobacter jejuni

Synonyms

Synonyms Comment Organism
QFR
-
 Helicobacter pylori
QFR
-
 Wolinella succinogenes
QFR
-
 Campylobacter jejuni
quinol:fumarate reductase
-
 Helicobacter pylori
quinol:fumarate reductase
-
 Wolinella succinogenes
quinol:fumarate reductase
-
 Campylobacter jejuni

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Helicobacter pylori
FAD
-
 Wolinella succinogenes
FAD
-
 Campylobacter jejuni
heme a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B Helicobacter pylori
heme a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B Wolinella succinogenes
heme a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B Campylobacter jejuni

General Information

General Information Comment Organism
additional information the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview Helicobacter pylori
additional information the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview Wolinella succinogenes
additional information the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview Campylobacter jejuni