2bcc
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The cytochrome bc1 is one of the three major respiratory enzyme complexes, residing in the inner mitochondrial membrane. Cytochrome bc1 transfers, electrons from ubiquinol to cytochrome c and uses the energy thus released, to form an electrochemical gradient across the inner membrane. Our X-ray, crystal structures of the complex from chicken, cow and rabbit in both the, presence and absence of inhibitors of quinone oxidation, reveal two, different locations for the extrinsic domain of one component of the, enzyme, an iron-sulphur protein. One location is close enough to the, supposed quinol oxidation site to allow reduction of the Fe-S protein by, ubiquinol. The other site is close enough to cytochrome c1 to allow, oxidation of the Fe-S protein by the cytochrome. As neither location will, .. | + | The cytochrome bc1 is one of the three major respiratory enzyme complexes, residing in the inner mitochondrial membrane. Cytochrome bc1 transfers, electrons from ubiquinol to cytochrome c and uses the energy thus released, to form an electrochemical gradient across the inner membrane. Our X-ray, crystal structures of the complex from chicken, cow and rabbit in both the, presence and absence of inhibitors of quinone oxidation, reveal two, different locations for the extrinsic domain of one component of the, enzyme, an iron-sulphur protein. One location is close enough to the, supposed quinol oxidation site to allow reduction of the Fe-S protein by, ubiquinol. The other site is close enough to cytochrome c1 to allow, oxidation of the Fe-S protein by the cytochrome. As neither location will, allow both reactions to proceed at a suitable rate, the reaction mechanism, must involve movement of the extrinsic domain of the Fe-S component in, order to shuttle electrons from ubiquinol to cytochrome c1. Such a, mechanism has not previously been observed in redox protein complexes. |
==About this Structure== | ==About this Structure== | ||
| - | 2BCC is a | + | 2BCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with BOG, HEM, FES, U10, PEE and SIG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Structure known Active Sites: BHI, BLO, C1H and FES. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BCC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubiquinone]] | [[Category: ubiquinone]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:54:00 2007'' |
Revision as of 11:48, 5 November 2007
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STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN
Overview
The cytochrome bc1 is one of the three major respiratory enzyme complexes, residing in the inner mitochondrial membrane. Cytochrome bc1 transfers, electrons from ubiquinol to cytochrome c and uses the energy thus released, to form an electrochemical gradient across the inner membrane. Our X-ray, crystal structures of the complex from chicken, cow and rabbit in both the, presence and absence of inhibitors of quinone oxidation, reveal two, different locations for the extrinsic domain of one component of the, enzyme, an iron-sulphur protein. One location is close enough to the, supposed quinol oxidation site to allow reduction of the Fe-S protein by, ubiquinol. The other site is close enough to cytochrome c1 to allow, oxidation of the Fe-S protein by the cytochrome. As neither location will, allow both reactions to proceed at a suitable rate, the reaction mechanism, must involve movement of the extrinsic domain of the Fe-S component in, order to shuttle electrons from ubiquinol to cytochrome c1. Such a, mechanism has not previously been observed in redox protein complexes.
About this Structure
2BCC is a Single protein structure of sequence from Gallus gallus with BOG, HEM, FES, U10, PEE and SIG as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Structure known Active Sites: BHI, BLO, C1H and FES. Full crystallographic information is available from OCA.
Reference
Electron transfer by domain movement in cytochrome bc1., Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH, Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029
Page seeded by OCA on Mon Nov 5 13:54:00 2007
Categories: Gallus gallus | Single protein | Ubiquinol--cytochrome-c reductase | Berry, E.A. | Chi, Y.I. | Crofts, A.R. | Huang, L. | Hung, L.W. | Kim, K.K. | Kim, S.H. | Shulmeister, V.M. | Zhang, Z. | BOG | FES | HEM | PEE | SIG | U10 | Membrane protein | Oxidoreductase | Redox enzyme | Respiratory chain | Stigmatellin | Ubiquinone
