Literature summary for 7.1.1.8 extracted from

Gao, X.; Wen, X.; Esser, L.; Quinn, B.; Yu, L.; Yu, C.A.; Xia, D.
Structural basis for the quinone reduction in the bc1 complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc1 with bound substrate and inhibitors at the Qi site (2003), Biochemistry, 42, 9067-9080.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified native oxidized enzyme complex or enzyme bound to antimycin A1 or 2-nonyl-4-hydroxyquinoline N-oxide, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM MOPS, pH 7.2, 20 mM ammonium acetate, 20% w/v glycerol, and either 0.1% decanoyl-N-methylglucamide or 0.1% diheptanoyl phosphatidylcholine, or 0.16% sucrose monocaprate, mixed with precipitant solution, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling	Bos taurus

Crystallization (Comment)

Organism

purified native oxidized enzyme complex or enzyme bound to antimycin A1 or 2-nonyl-4-hydroxyquinoline N-oxide, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM MOPS, pH 7.2, 20 mM ammonium acetate, 20% w/v glycerol, and either 0.1% decanoyl-N-methylglucamide or 0.1% diheptanoyl phosphatidylcholine, or 0.16% sucrose monocaprate, mixed with precipitant solution, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling

Bos taurus

Inhibitors

Inhibitors	Comment	Organism
2-nonyl-4-hydroxyquinoline N-oxide	binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview	Bos taurus
antimycin A1	binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview	Bos taurus
additional information	structure determination of the inhibitor binding site Qi, located near the matrix side of the membrane bilayer	Bos taurus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	integral	Bos taurus	16020	-
mitochondrion	-	Bos taurus	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Bos taurus	enzyme is a central component of cellular energy conservation machinery	?	-	?
ubiquinol-2 + 2 ferricytochrome c	Bos taurus	enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes	ubiquinone-2 + 2 ferrocytochrome c + 2 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
fully oxidized enzyme complex to homogeneity	Bos taurus

Reaction

Reaction	Comment	Organism	Reaction ID
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	substrate binding site Qo structure, conformational changes upon inhibitor binding, overview	Bos taurus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Bos taurus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	enzyme is a central component of cellular energy conservation machinery	Bos taurus	?	-	?
ubiquinol-2 + 2 ferricytochrome c	enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes	Bos taurus	ubiquinone-2 + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol-2 + 2 ferricytochrome c	binding interaction of ubiquinone with cytochrome b, overview	Bos taurus	ubiquinone-2 + 2 ferrocytochrome c + 2 H+	-	?

Subunits

Subunits	Comment	Organism
dimer	enzyme complex	Bos taurus

Synonyms

Synonyms	Comment	Organism
Cyt bc1 complex	-	Bos taurus
cytochrome bc1 complex	-	Bos taurus
quinol cyt. c oxidoreductase (bc1)	-	Bos taurus