Cytochrome bc1 complex
From Proteopedia
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| - | <StructureSection load='1zrt' size='350' side='right' caption='Cytochrome bc1 containing Cb (pink, neon green), Cc1 (yellow, sea green), RISP (magenta, blue) and Fe2S2 complex with stigmatellin (PDB entry [[1zrt]])' scene=''> | + | <StructureSection load='1zrt' size='350' side='right' caption='Cytochrome bc1 containing Cb (pink, neon green), Cc1 (yellow, sea green), RISP (magenta, blue) and Fe2S2 complex with stigmatellin (PDB entry [[1zrt]])' scene='49/490879/Cv/1'> |
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'''Cytochrome bc1''' (Cbc1) functions as the central pump which transfers protons across the cell membrane. The protons are used to power the rotation of ATP synthase. Cbc1 binds ubiquinol which carries hydrogen atoms. Cbc1 separates the protons and the electrons. The protons are released in the inner side of the membrane for use by ATP synthase and the electrons are transferred to cytochrome c or to the outer side of the membrane. Plants use '''cytochrome b6f''' in the same manner binding plastoquinol as a hydrogen carrier. Stigmatellin inhibits the Cbc1 electron transfer by binding to its quinone oxidation site. Antimycin inhibits Cbc1 by binding to its quinone reduction site.<ref>PMID:14977419</ref> | '''Cytochrome bc1''' (Cbc1) functions as the central pump which transfers protons across the cell membrane. The protons are used to power the rotation of ATP synthase. Cbc1 binds ubiquinol which carries hydrogen atoms. Cbc1 separates the protons and the electrons. The protons are released in the inner side of the membrane for use by ATP synthase and the electrons are transferred to cytochrome c or to the outer side of the membrane. Plants use '''cytochrome b6f''' in the same manner binding plastoquinol as a hydrogen carrier. Stigmatellin inhibits the Cbc1 electron transfer by binding to its quinone oxidation site. Antimycin inhibits Cbc1 by binding to its quinone reduction site.<ref>PMID:14977419</ref> | ||
Revision as of 11:38, 22 December 2015
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3D structures of cytochrome bc1
Updated on 22-December-2015
2fyn - RsCb (mutant) + Cc1 + RISP – Rhodobacter sphaeroides
1zrt - Cb + Cc1 + RISP – Rhodobacter capsulatus
1bgy, 1be3, 1l0n, 1ntm - bCb + bCc1 + RISP – bovine
1qcr - bCb + bCc1 + RISP – Cα model
1sqp, 2fyu, 1l0l, 1ntk, 1pp9, 1ppj, 1sqb, 2a06, 1sqv, 1sqx, 1sqq - bCb + bCc1 + RISP + inhibitor
4d6u - bCb + bCc1 + RISP + antimalarial pyridone
1ntz - bCb + bCc1 + RISP + ubiquinone
1nu1 - bCb + bCc1 + RISP + quinolone derivative
2qjk - RsCb (mutant) + RsCc1 + RISP + inhibitor
2qjp - RsCb + RsCc1 + RISP + inhibitor
2qjy - RsCb (mutant) + RsCc1 + RISP (mutant) + inhibitor
2ibz, 1kyo, 1kb9, 1p84 - yCb + yCc1 + RISP + inhibitor - yeast
3cx5 - yCb + yCc1 + RISP
1ezv - yCb + yCc1 + RISP + antibody
2yiu - Cb + Cc1 + RISP – Paracoccus denitrificans
1qcr - bCb + bCc1 + RISP – bovine – Cα model
3cxh, 3h1h, 1bcc, 3h1h - cCb + cCc1 + RISP - chicken
3cwb, 3h1i, 3h1j, 3h1k, 3h1l, 3l70, 3l71, 3l72, 3l73, 3l74, 3l75, 3tgu, 3bcc, 2bcc, 3h1i - cCb + cCc1 + RISP + inhibitor
References
- ↑ Crofts AR. The cytochrome bc1 complex: function in the context of structure. Annu Rev Physiol. 2004;66:689-733. PMID:14977419 doi:http://dx.doi.org/10.1146/annurev.physiol.66.032102.150251
- ↑ Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, Daldal F. X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts. Photosynth Res. 2004;81(3):251-75. PMID:16034531 doi:http://dx.doi.org/10.1023/B:PRES.0000036888.18223.0e
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