Literature summary for 7.1.1.8 extracted from

Xia, D.; Esser, L.; Tang, W.K.; Zhou, F.; Zhou, Y.; Yu, L.; Yu, C.A.
Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function (2013), Biochim. Biophys. Acta, 1827, 1278-1294.

Activating Compound

Activating Compound	Comment	Organism
additional information	cardiolipin is essential for the function of bc1	Gallus gallus
additional information	cardiolipin is essential for the function of bc1	Bos taurus
additional information	cardiolipin is essential for the function of bc1	Spinacia oleracea
additional information	cardiolipin is essential for the function of bc1. Two phosphatidylethanolamines, one phosphatidylcholine, one phosphatidyinositol, and one cardiolipin are bound to the enzyme cmplex	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
bc1 crystal structure analysis	Gallus gallus
bc1 crystal structure analysis	Paracoccus denitrificans
bc1 crystal structure analysis	Bos taurus
bc1 crystal structure analysis	Spinacia oleracea
bc1 crystal structure analysis	Rhodobacter capsulatus
bc1 from Rhodobacter sphaeroides can only be crystallized bound to certain types of inhibitors such as stigmatellin and famoxadone, bc1 crystal structure analysis	Cereibacter sphaeroides
crystallized in the presence of stigmatellin or hexahydrodibenzothiophene, bc1 crystal structure analysis	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole	-	Bos taurus
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole	-	Cereibacter sphaeroides
antimycin A	-	Bos taurus
antimycin A	-	Cereibacter sphaeroides
antimycin A	-	Gallus gallus
antimycin A	-	Paracoccus denitrificans
antimycin A	-	Rhodobacter capsulatus
antimycin A	-	Saccharomyces cerevisiae
antimycin A	-	Spinacia oleracea
famoxadone	-	Cereibacter sphaeroides
additional information	ubiquinol cannot act as inhibitor	Bos taurus
additional information	ubiquinol cannot act as inhibitor	Cereibacter sphaeroides
Myxothiazol	-	Bos taurus
Myxothiazol	-	Cereibacter sphaeroides
Stigmatellin	-	Cereibacter sphaeroides
Zn2+	crystalline chicken bc1 complex specifically binds Zn2+ ions at two identical sites or one per monomer in the dimer. Zinc binding occurs close to the QP site and is likely to be the reason for the inhibitory effect on the activity of bc1 observable during zinc titration. The Zn2+ ion binds to a hydrophilic area between cytochromes b and c1 and is coordinated by GgH212 of cyt c1, GgH268, GgD253, and GgE255 of cyt b, and might interfere with the egress of protons from the QP site to the intermembrane aqueous medium. No Zn2+ is bound at the zinc binding motif of the putative MPP active site of core-1 and core-2 for chicken bc1 after prolonged soaking	Gallus gallus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Gallus gallus	16020	-
membrane	-	Paracoccus denitrificans	16020	-
membrane	-	Saccharomyces cerevisiae	16020	-
membrane	-	Bos taurus	16020	-
membrane	-	Cereibacter sphaeroides	16020	-
membrane	-	Spinacia oleracea	16020	-
membrane	-	Rhodobacter capsulatus	16020	-
mitochondrion	-	Gallus gallus	5739	-
mitochondrion	-	Saccharomyces cerevisiae	5739	-
mitochondrion	-	Bos taurus	5739	-
mitochondrion	-	Spinacia oleracea	5739	-

Metals/Ions

Metals/Ions	Comment	Organism
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Gallus gallus
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Paracoccus denitrificans
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Saccharomyces cerevisiae
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Bos taurus
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Cereibacter sphaeroides
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Spinacia oleracea
Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	Rhodobacter capsulatus
additional information	no Zn2+ in the native enzyme structure	Saccharomyces cerevisiae
additional information	no Zn2+ in the native enzyme structure. No Sr2+ binding sites in mitochondrial bc1	Bos taurus
Sr2+	conserved binding site in photosynthetic bacteria is on cyt c1	Rhodobacter capsulatus
Sr2+	crystals of Rsbc1 grown in the presence of strontium ions reveal several Sr2+ binding sites. One site that is not present in mitochondrial bc1 but appears to be conserved in photosynthetic bacteria is on cyt c1	Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
ubiquinol + 2 ferricytochrome c	Paracoccus denitrificans	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Cereibacter sphaeroides	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Rhodobacter capsulatus	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Gallus gallus	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Saccharomyces cerevisiae	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Bos taurus	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	Spinacia oleracea	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-
Cereibacter sphaeroides	-	-	-
Gallus gallus	-	-	-
Paracoccus denitrificans	-	-	-
Rhodobacter capsulatus	-	-	-
Saccharomyces cerevisiae	-	-	-
Spinacia oleracea	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Gallus gallus	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Paracoccus denitrificans	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Saccharomyces cerevisiae	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Bos taurus	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Cereibacter sphaeroides	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Spinacia oleracea	a
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]	reaction mechanism, structure-function analysis, overview	Rhodobacter capsulatus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Bos taurus	-
leaf	-	Spinacia oleracea	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ubiquinol + 2 ferricytochrome c	-	Gallus gallus	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Paracoccus denitrificans	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Saccharomyces cerevisiae	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Cereibacter sphaeroides	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Spinacia oleracea	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Rhodobacter capsulatus	ubiquinone + 2 ferrocytochrome c + 2 H+	-	?
ubiquinol + 2 ferricytochrome c	-	Bos taurus	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	Paracoccus denitrificans	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	Cereibacter sphaeroides	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced	Rhodobacter capsulatus	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	Gallus gallus	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	Saccharomyces cerevisiae	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	Bos taurus	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?
ubiquinol + 2 ferricytochrome c	the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site	Spinacia oleracea	ubiquinone + 2 ferrocytochrome c + 2 H+	interaction with ubiquinone at the QN site, overview	?

Subunits

Subunits	Comment	Organism
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Gallus gallus
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Paracoccus denitrificans
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Saccharomyces cerevisiae
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Bos taurus
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Cereibacter sphaeroides
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Spinacia oleracea
More	structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview	Rhodobacter capsulatus

Synonyms

Synonyms	Comment	Organism
bc1	-	Gallus gallus
bc1	-	Paracoccus denitrificans
bc1	-	Saccharomyces cerevisiae
bc1	-	Bos taurus
bc1	-	Cereibacter sphaeroides
bc1	-	Spinacia oleracea
bc1	-	Rhodobacter capsulatus
complex III	-	Gallus gallus
complex III	-	Paracoccus denitrificans
complex III	-	Saccharomyces cerevisiae
complex III	-	Bos taurus
complex III	-	Cereibacter sphaeroides
complex III	-	Spinacia oleracea
complex III	-	Rhodobacter capsulatus
cyt bc1	-	Gallus gallus
cyt bc1	-	Paracoccus denitrificans
cyt bc1	-	Saccharomyces cerevisiae
cyt bc1	-	Bos taurus
cyt bc1	-	Cereibacter sphaeroides
cyt bc1	-	Spinacia oleracea
cyt bc1	-	Rhodobacter capsulatus
cytochrome bc	-	Gallus gallus
cytochrome bc	-	Paracoccus denitrificans
cytochrome bc	-	Saccharomyces cerevisiae
cytochrome bc	-	Bos taurus
cytochrome bc	-	Cereibacter sphaeroides
cytochrome bc	-	Spinacia oleracea
cytochrome bc	-	Rhodobacter capsulatus
ubiquinol cytochrome c oxidoreductase	-	Gallus gallus
ubiquinol cytochrome c oxidoreductase	-	Paracoccus denitrificans
ubiquinol cytochrome c oxidoreductase	-	Saccharomyces cerevisiae
ubiquinol cytochrome c oxidoreductase	-	Bos taurus
ubiquinol cytochrome c oxidoreductase	-	Cereibacter sphaeroides
ubiquinol cytochrome c oxidoreductase	-	Spinacia oleracea
ubiquinol cytochrome c oxidoreductase	-	Rhodobacter capsulatus

General Information

General Information	Comment	Organism
malfunction	the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced	Gallus gallus
malfunction	the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced	Saccharomyces cerevisiae
malfunction	the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced	Bos taurus
malfunction	the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced	Spinacia oleracea
metabolism	the complex III also exhibits enzyme mitochondrial processing peptidase activity	Gallus gallus
metabolism	the complex III also exhibits enzyme mitochondrial processing peptidase activity	Saccharomyces cerevisiae
metabolism	the complex III also exhibits enzyme mitochondrial processing peptidase activity	Spinacia oleracea
metabolism	the complex III also exhibits enzyme mitochondrial processing peptidase activity, which is inactive in bovine cells, but can be activated through detergents treatment	Bos taurus
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Bos taurus
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Cereibacter sphaeroides
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Rhodobacter capsulatus
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Paracoccus denitrificans
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Gallus gallus
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Saccharomyces cerevisiae
additional information	the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions	Spinacia oleracea
physiological function	respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview	Gallus gallus
physiological function	respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview	Saccharomyces cerevisiae
physiological function	respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview	Bos taurus
physiological function	respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview	Spinacia oleracea
physiological function	respiratory complex III is an electron transport complex, related bc complexes, overview	Paracoccus denitrificans
physiological function	respiratory complex III is an electron transport complex, related bc complexes, overview	Cereibacter sphaeroides
physiological function	respiratory complex III is an electron transport complex, related bc complexes, overview	Rhodobacter capsulatus