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Literature summary extracted from
- Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function (2013), Biochim. Biophys. Acta, 1827, 1278-1294.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | additional information | cardiolipin is essential for the function of bc1 | Gallus gallus | |
| 7.1.1.8 | additional information | cardiolipin is essential for the function of bc1 | Bos taurus | |
| 7.1.1.8 | additional information | cardiolipin is essential for the function of bc1 | Spinacia oleracea | |
| 7.1.1.8 | 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)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.1.1.8 | bc1 crystal structure analysis | Gallus gallus |
| 7.1.1.8 | bc1 crystal structure analysis | Paracoccus denitrificans |
| 7.1.1.8 | bc1 crystal structure analysis | Bos taurus |
| 7.1.1.8 | bc1 crystal structure analysis | Spinacia oleracea |
| 7.1.1.8 | bc1 crystal structure analysis | Rhodobacter capsulatus |
| 7.1.1.8 | 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 |
| 7.1.1.8 | crystallized in the presence of stigmatellin or hexahydrodibenzothiophene, bc1 crystal structure analysis | Saccharomyces cerevisiae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | 5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole | - |
Bos taurus |  |
| 7.1.1.8 | 5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole | - |
Cereibacter sphaeroides | |
| 7.1.1.8 | antimycin A | - |
Bos taurus | |
| 7.1.1.8 | antimycin A | - |
Cereibacter sphaeroides | |
| 7.1.1.8 | antimycin A | - |
Gallus gallus | |
| 7.1.1.8 | antimycin A | - |
Paracoccus denitrificans | |
| 7.1.1.8 | antimycin A | - |
Rhodobacter capsulatus | |
| 7.1.1.8 | antimycin A | - |
Saccharomyces cerevisiae | |
| 7.1.1.8 | antimycin A | - |
Spinacia oleracea | |
| 7.1.1.8 | famoxadone | - |
Cereibacter sphaeroides | |
| 7.1.1.8 | additional information | ubiquinol cannot act as inhibitor | Bos taurus | |
| 7.1.1.8 | additional information | ubiquinol cannot act as inhibitor | Cereibacter sphaeroides | |
| 7.1.1.8 | Myxothiazol | - |
Bos taurus | |
| 7.1.1.8 | Myxothiazol | - |
Cereibacter sphaeroides | |
| 7.1.1.8 | Stigmatellin | - |
Cereibacter sphaeroides | |
| 7.1.1.8 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.8 | membrane | - |
Gallus gallus | 16020 | - |
| 7.1.1.8 | membrane | - |
Paracoccus denitrificans | 16020 | - |
| 7.1.1.8 | membrane | - |
Saccharomyces cerevisiae | 16020 | - |
| 7.1.1.8 | membrane | - |
Bos taurus | 16020 | - |
| 7.1.1.8 | membrane | - |
Cereibacter sphaeroides | 16020 | - |
| 7.1.1.8 | membrane | - |
Spinacia oleracea | 16020 | - |
| 7.1.1.8 | membrane | - |
Rhodobacter capsulatus | 16020 | - |
| 7.1.1.8 | mitochondrion | - |
Gallus gallus | 5739 | - |
| 7.1.1.8 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
| 7.1.1.8 | mitochondrion | - |
Bos taurus | 5739 | - |
| 7.1.1.8 | mitochondrion | - |
Spinacia oleracea | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Gallus gallus | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Paracoccus denitrificans | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Saccharomyces cerevisiae | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Bos taurus | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Cereibacter sphaeroides | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Spinacia oleracea | |
| 7.1.1.8 | Fe2+ | iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview | Rhodobacter capsulatus | |
| 7.1.1.8 | additional information | no Zn2+ in the native enzyme structure | Saccharomyces cerevisiae | |
| 7.1.1.8 | additional information | no Zn2+ in the native enzyme structure. No Sr2+ binding sites in mitochondrial bc1 | Bos taurus | |
| 7.1.1.8 | Sr2+ | conserved binding site in photosynthetic bacteria is on cyt c1 | Rhodobacter capsulatus | |
| 7.1.1.8 | 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)
| 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 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.8 | Bos taurus | - |
- |
- |
| 7.1.1.8 | Cereibacter sphaeroides | - |
- |
- |
| 7.1.1.8 | Gallus gallus | - |
- |
- |
| 7.1.1.8 | Paracoccus denitrificans | - |
- |
- |
| 7.1.1.8 | Rhodobacter capsulatus | - |
- |
- |
| 7.1.1.8 | Saccharomyces cerevisiae | - |
- |
- |
| 7.1.1.8 | Spinacia oleracea | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Gallus gallus | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Paracoccus denitrificans | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Saccharomyces cerevisiae | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Bos taurus | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Cereibacter sphaeroides | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Spinacia oleracea | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism, structure-function analysis, overview | Rhodobacter capsulatus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.1.1.8 | heart | - |
Bos taurus | - |
| 7.1.1.8 | leaf | - |
Spinacia oleracea | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Gallus gallus | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Paracoccus denitrificans | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Saccharomyces cerevisiae | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Cereibacter sphaeroides | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Spinacia oleracea | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Rhodobacter capsulatus | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Bos taurus | ubiquinone + 2 ferrocytochrome c + 2 H+ | interaction with ubiquinone at the QN site, overview | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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 | ? | |
| 7.1.1.8 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Gallus gallus |
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Paracoccus denitrificans |
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Saccharomyces cerevisiae |
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Bos taurus |
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Cereibacter sphaeroides |
| 7.1.1.8 | More | structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview | Spinacia oleracea |
| 7.1.1.8 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | bc1 | - |
Gallus gallus |
| 7.1.1.8 | bc1 | - |
Paracoccus denitrificans |
| 7.1.1.8 | bc1 | - |
Saccharomyces cerevisiae |
| 7.1.1.8 | bc1 | - |
Bos taurus |
| 7.1.1.8 | bc1 | - |
Cereibacter sphaeroides |
| 7.1.1.8 | bc1 | - |
Spinacia oleracea |
| 7.1.1.8 | bc1 | - |
Rhodobacter capsulatus |
| 7.1.1.8 | complex III | - |
Gallus gallus |
| 7.1.1.8 | complex III | - |
Paracoccus denitrificans |
| 7.1.1.8 | complex III | - |
Saccharomyces cerevisiae |
| 7.1.1.8 | complex III | - |
Bos taurus |
| 7.1.1.8 | complex III | - |
Cereibacter sphaeroides |
| 7.1.1.8 | complex III | - |
Spinacia oleracea |
| 7.1.1.8 | complex III | - |
Rhodobacter capsulatus |
| 7.1.1.8 | cyt bc1 | - |
Gallus gallus |
| 7.1.1.8 | cyt bc1 | - |
Paracoccus denitrificans |
| 7.1.1.8 | cyt bc1 | - |
Saccharomyces cerevisiae |
| 7.1.1.8 | cyt bc1 | - |
Bos taurus |
| 7.1.1.8 | cyt bc1 | - |
Cereibacter sphaeroides |
| 7.1.1.8 | cyt bc1 | - |
Spinacia oleracea |
| 7.1.1.8 | cyt bc1 | - |
Rhodobacter capsulatus |
| 7.1.1.8 | cytochrome bc | - |
Gallus gallus |
| 7.1.1.8 | cytochrome bc | - |
Paracoccus denitrificans |
| 7.1.1.8 | cytochrome bc | - |
Saccharomyces cerevisiae |
| 7.1.1.8 | cytochrome bc | - |
Bos taurus |
| 7.1.1.8 | cytochrome bc | - |
Cereibacter sphaeroides |
| 7.1.1.8 | cytochrome bc | - |
Spinacia oleracea |
| 7.1.1.8 | cytochrome bc | - |
Rhodobacter capsulatus |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Gallus gallus |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Paracoccus denitrificans |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Saccharomyces cerevisiae |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Bos taurus |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Cereibacter sphaeroides |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Spinacia oleracea |
| 7.1.1.8 | ubiquinol cytochrome c oxidoreductase | - |
Rhodobacter capsulatus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | metabolism | the complex III also exhibits enzyme mitochondrial processing peptidase activity | Gallus gallus |
| 7.1.1.8 | metabolism | the complex III also exhibits enzyme mitochondrial processing peptidase activity | Saccharomyces cerevisiae |
| 7.1.1.8 | metabolism | the complex III also exhibits enzyme mitochondrial processing peptidase activity | Spinacia oleracea |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | 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 |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview | Gallus gallus |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview | Saccharomyces cerevisiae |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview | Bos taurus |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview | Spinacia oleracea |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex, related bc complexes, overview | Paracoccus denitrificans |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex, related bc complexes, overview | Cereibacter sphaeroides |
| 7.1.1.8 | physiological function | respiratory complex III is an electron transport complex, related bc complexes, overview | Rhodobacter capsulatus |
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Release 2023.1 (January 2023)
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