Literature summary for 7.1.1.8 extracted from

Ritter, M.; Anderka, O.; Ludwig, B.; Mantele, W.; Hellwig, P.
Electrochemical and FTIR spectroscopic characterization of the cytochrome bc1 complex from Paracoccus denitrificans: evidence for protonation reactions coupled to quinone binding (2003), Biochemistry, 42, 12391-12399.

Search for more literature for 7.1.1.8

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	enzyme contains 2 cytochromes with heme groups, enzyme contains a Rieske [2Fe-2S] cluster, structure analysis of the Rieske ISP and of soluble fragments thereof	Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ubiquinol-2 + 2 ferricytochrome c	Paracoccus denitrificans	-	ubiquinone-2 + 2 ferrocytochrome c + 2 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of cytochrome c1, and the Rieske ISP with soluble fragments	Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	protonation reactions coupled to quinone binding, binding of 2.3-2.6 quinones per enzyme monomer at the Qo side, conformational changes	Paracoccus denitrificans	?	-	?
ubiquinol-2 + 2 ferricytochrome c	-	Paracoccus denitrificans	ubiquinone-2 + 2 ferrocytochrome c + 2 H+	-	?

Subunits

Subunits	Comment	Organism
More	spectroscopic enzyme complex composition analysis, structural changes upon cofactor or substrate binding, overview	Paracoccus denitrificans

Synonyms

Synonyms	Comment	Organism
cytochrome bc1 complex	-	Paracoccus denitrificans

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome c1	-	Paracoccus denitrificans

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Release 2023.1 (January 2023)