Journal
BIOCHEMISTRY
Volume 52, Issue 15, Pages 2649-2654Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi301638h
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Funding
- National Institutes of Health [GM-038323]
- Henry Koffler Distinguished Professorship
- Purdue University
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Cytochrome b(6)f catalyzes quinone redox reactions within photosynthetic membranes to generate a transmembrane proton electrochemical gradient for ATP synthesis. A key step involves the transfer of an electron from the [2Fe-2S] cluster of the iron-sulfur protein (ISP) extrinsic domain to the cytochrome f heme across a distance of 26 angstrom, which is too large for competent electron transfer but could be bridged by translation-rotation of the ISP. Here we report the first crystallographic evidence of significant motion of the ISP extrinsic domain. It is inferred that extensive crystallographic disorder of the ISP extrinsic domain indicates conformational flexibility. The ISP disorder observed in this structure, in contrast to the largely ordered ISP structure observed in the b(6)f complex supplemented with neutral lipids, is attributed to electrostatic interactions arising from anionic lipids.
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