3bcc

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spinqualitylabelsall models 3bcc, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STIGMATELLIN AND ANTIMYCIN 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

3BCC is a Protein complex structure of sequences from Gallus gallus with HEM, FES, SIG and AMY as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 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

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