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Published Online October 2, 2003
Science DOI: 10.1126/science.1090165

Research Articles

Submitted on August 6, 2003
Accepted on September 24, 2003

Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity

Genji Kurisu 1, Huamin Zhang 2, Janet L. Smith 2, William A. Cramer 2*

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

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

The cytochrome b6f complex provides the electronic connection between the photosystem I and photosystem II reaction centers of oxygenic photosynthesis and generates a trans-membrane electrochemical proton gradient for ATP synthesis. A 3.0-Å 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 analogue 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.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)