Literature summary extracted from
Kleinschroth, T.; Castellani, M.; Trinh, C.H.; Morgner, N.; Brutschy, B.; Ludwig, B.; Hunte, C.
X-ray structure of the dimeric cytochrome bc1 complex from the soil bacterium Paracoccus denitrificans at 2.7-A resolution (2011), Biochim. Biophys. Acta, 1807, 1606-1615.
Application
EC Number |
Application |
Comment |
Organism |
---|
7.1.1.8 |
additional information |
the complex from the alpha-proteobacterium Paracoccus denitrificans is a model for the medically relevant mitochondrial complexes |
Paracoccus denitrificans |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
7.1.1.8 |
recombinant expression of cyt bc1DELTAac complex fused with a C-terminal deca-histidine-tag at cyt b |
Paracoccus denitrificans |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
7.1.1.8 |
purified recombinant fully functional complex, hanging drop vapour diffusion method, 20 mg/ml protein in 25 mM sodium phosphate, pH 7.5, 250 mM NaCl and 0.02% beta-ddodecyl-malto-pyranoside is mixed with reservoir solution, containing 100 mM sodium acetate, pH 4.6, 50 mM NaCl, 33% 2-methyl-2,4-pentandiol, in a 1:2 ratio, 18°C, 4 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement |
Paracoccus denitrificans |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
7.1.1.8 |
additional information |
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer |
Paracoccus denitrificans |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
Stigmatellin |
species-specific binding of the inhibitor, binding structure and mechanism, overview |
Paracoccus denitrificans |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
Fe2+ |
Rieske protein, the subunit iron-sulfur protein is made up of three domains. The membrane anchor is an N-terminal TMH (Asp17-Gln41) with pronounced tilt which brings the catalytic domain in contact with the second monomer providing the structural basis for the functional dimer. The catalytic domain is interconnected with the TMH by the hinge region, Met42-Leu51, which harbours the ADV motif, Ala46-Val48 |
Paracoccus denitrificans |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
7.1.1.8 |
ubiquinol + 2 ferricytochrome c |
Paracoccus denitrificans |
- |
ubiquinone + 2 ferrocytochrome c + 2 H+ |
- |
? |
|
7.1.1.8 |
ubiquinol + 2 ferricytochrome c552 |
Paracoccus denitrificans |
- |
ubiquinone + 2 ferrocytochrome c552 + 2 H+ |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
7.1.1.8 |
Paracoccus denitrificans |
P05418 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
7.1.1.8 |
ubiquinol + 2 ferricytochrome c |
- |
Paracoccus denitrificans |
ubiquinone + 2 ferrocytochrome c + 2 H+ |
- |
? |
|
7.1.1.8 |
ubiquinol + 2 ferricytochrome c552 |
- |
Paracoccus denitrificans |
ubiquinone + 2 ferrocytochrome c552 + 2 H+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
7.1.1.8 |
dimer |
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer |
Paracoccus denitrificans |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
7.1.1.8 |
cyt bc1 |
- |
Paracoccus denitrificans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
cytochrome b |
two cyt b subunits form the hydrophobic core of the complex, overview |
Paracoccus denitrificans |
|
7.1.1.8 |
cytochrome c1 |
the domain houses the cofactor heme c1 which is bound by the characteristic CXXCH motif with residues Cys82, Cys85, His86 (Cys245cyt c1, Cys248cyt c1, His249cyt c1) and with Met210 (Met373cyt c1) as the sixth heme ligand, structure of the subunit, overview |
Paracoccus denitrificans |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
7.1.1.8 |
additional information |
structural diversity in the cytochrome c1 surface facing the iron-sulfur protein domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. Modelling of the electron transfer complex with membrane-anchored cytochrome c552, the natural substrate |
Paracoccus denitrificans |
7.1.1.8 |
physiological function |
the respiratory cytochrome bc1 complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of protonmotive force which fuels ATP synthesis |
Paracoccus denitrificans |