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Literature summary for 1.3.5.1 extracted from

  • Xin, Y.; Lu, Y.K.; Fromme, R.; Fromme, P.; Blankenship, R.E.
    Purification, characterization and crystallization of menaquinol:fumarate oxidoreductase from the green filamentous photosynthetic bacterium Chloroflexus aurantiacus (2009), Biochim. Biophys. Acta, 1787, 86-96.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction data up to 3.2 Å resolution Chloroflexus aurantiacus

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: heptyl 4-hydroxyquinoline N-oxide Chloroflexus aurantiacus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane cytoplasmic membrane Chloroflexus aurantiacus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes Chloroflexus aurantiacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27097
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
27097
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
28064
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
28064
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
73234
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
73234
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
260000
-
Blue-native PAGE Chloroflexus aurantiacus

Organism

Organism UniProt Comment Textmining
Chloroflexus aurantiacus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Chloroflexus aurantiacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + reduced phenazine methosulfate enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities Chloroflexus aurantiacus succinate + phenazine methosulfate
-
r
succinate + menaquinone
-
Chloroflexus aurantiacus fumarate + menaquinol
-
r
succinate + phenazine methosulfate enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities Chloroflexus aurantiacus fumarate + reduced phenazine methosulfate
-
r

Subunits

Subunits Comment Organism
? 1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus
? 1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones Chloroflexus aurantiacus

Synonyms

Synonyms Comment Organism
menaquinol:fumarate oxidoreductase
-
Chloroflexus aurantiacus
mQFR
-
Chloroflexus aurantiacus

Cofactor

Cofactor Comment Organism Structure
FAD stoichiometric ratio between covalently bound FAD and the iron-sulfur cluster is 1:1. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD Chloroflexus aurantiacus
heme enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD Chloroflexus aurantiacus
iron-sulfur centre enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. The purified mQFR complex has two iron-sulfur centers of the ferredoxin type that are paramagnetic in the reduced state, 2Fe-2S and 4Fe-4S, and one iron-sulfur center of the high potential type that is paramagnetic in the oxidized state, 3Fe-4S. Centers 2Fe-2S and 4Fe-4S exhibit a large difference in their redox midpoint potential, center 2Fe-2S is reducible with succinate, whereas the latter one can only be reduced by very low potential reductant such as dithionite Chloroflexus aurantiacus
phenazine methosulfate
-
Chloroflexus aurantiacus