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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{dagger}

The cytochrome b6f 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 b6f 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 b6f complex is similar to the analogous respiratory cytochrome bc1 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 b6f complex.

1 Department of Biological Sciences, 915 West State Street, Purdue University, West Lafayette, IN 47907–2054, USA.
2 Institute for Protein Research, Osaka University, Suita, Osaka 565–0871, Japan.


* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: wac{at}bilbo.bio.purdue.edu

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