An electronic bus bar lies in the core of cytochrome bc1.
An electronic bus bar lies in the core of cytochrome bc1.
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DOI:
10.1126/science.1190899
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发表时间:
2010-07-23
期刊:
影响因子:
--
通讯作者:
Osyczka A
中科院分区:
文献类型:
--
作者:
Swierczek M;Cieluch E;Sarewicz M;Borek A;Moser CC;Dutton PL;Osyczka A
The ubiquinol–cytochrome c oxidoreductases, central to cellular respiration and photosynthesis, are homodimers. High symmetry has frustrated resolution of whether cross-dimer interactions are functionally important. This has resulted in a proliferation of contradictory models. Here, we duplicated and fused cytochrome b subunits, and then broke symmetry by introducing independent mutations into each monomer. Electrons moved freely within and between monomers, crossing an electron-transfer bridge between two hemes in the core of the dimer. This revealed an H-shaped electron-transfer system that distributes electrons between four quinone oxidation-reduction terminals at the corners of the dimer within the millisecond time scale of enzymatic turnover. Free and unregulated distribution of electrons acts like a molecular-scale bus bar, a design often exploited in electronics.
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