X-ray crystallographic studies of the cytochrome bc1 complex
Abstract
Scope and Method of Study: The purpose of this study was to enhance the understanding of the bc1 complex. The method used in this study is x-ray crystallography and protein crystallization. Findings and Conclusion: The bc1 complex is an integral component of the electron transfer chain responsible for aiding in the production of a proton gradient for ATP synthesis. Mutations in the bc1 complex are associated with epilepsy and other human diseases. Functioning of the bc1 complex is commonly explained by the proton motive Q cycle. The proton motive Q cycle hypothesis makes use of only two completely separate substrate binding sites in the bc1 complex. Crystallographic anomalous signal tracking allowed for the deciphering of a hidden third substrate binding site which may have possible implications on the electron transferring pathway in the bc1 complex. A modified Q-cycle mechanism is proposed that makes use of the third substrate binding site.
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