Structure of the Cytochrome b 6 f Complex of Oxygenic Photosynthesis: Tuning the Cavity

Author:

Kurisu Genji12,Zhang Huamin12,Smith Janet L.12,Cramer William A.12

Affiliation:

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.

Abstract

The cytochrome b 6 f 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 6 f 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 6 f 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 6 f complex.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference43 articles.

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4. Oxygenic Photosynthesis: The Light Reactions 1996

5. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution

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