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Originally published in Science Express on 2 October 2003
Science 7 November 2003: Vol. 302. no. 5647, pp. 1009 - 1014
DOI: 10.1126/science.1090165
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Research Articles
Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
Genji Kurisu,1,2*
Huamin Zhang,1*
Janet L. Smith,1
William A. Cramer1
The cytochrome b 6f complex provides the electronic connection between the photosystem I and photosystem II reaction centers of oxygenic photosynthesis and generates a transmembrane electrochemical proton gradient for adenosine triphosphate synthesis. A 3.0 angstrom crystal structure of the dimeric b 6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quinone-analog inhibitor, and a novel heme are bound. The core of the b 6f complex is similar to the analogous respiratory cytochrome bc 1 complex, but the domain arrangement outside the core and the complement of prosthetic groups are strikingly different. The motion of the Rieske iron-sulfur protein extrinsic domain, essential for electron transfer, must also be different in the b 6f complex.
1 Department of Biological Sciences, 915 West State Street, Purdue University, West Lafayette, IN 479072054, USA.
2 Institute for Protein Research, Osaka University, Suita, Osaka 5650871, Japan.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: wac{at}bilbo.bio.purdue.edu
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