3bcc

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[[Image:3bcc.jpg|left|200px]]
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{{Seed}}
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[[Image:3bcc.png|left|200px]]
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{{STRUCTURE_3bcc| PDB=3bcc | SCENE= }}
{{STRUCTURE_3bcc| PDB=3bcc | SCENE= }}
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'''STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN'''
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===STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9565029 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9565029}}
==About this Structure==
==About this Structure==
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[[Category: Stigmatellin]]
[[Category: Stigmatellin]]
[[Category: Ubiquinone]]
[[Category: Ubiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:37:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:02:21 2008''

Revision as of 23:02, 27 July 2008

Template:STRUCTURE 3bcc

STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

Template:ABSTRACT PUBMED 9565029

About this Structure

3BCC is a Protein complex structure of sequences from Gallus gallus. 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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