Abstract
Photosynthetic reaction centers are membrane-bound pigment-protein complexes that use light to catalyze a transmembrane electron transfer against a steep thermodynamic gradient. They are found in plants and photosynthetic bacteria, and have evolved into two types. Type II reaction centers employ a mobile quinone as the terminal electron acceptor. Type I reaction centers employ an interpolypeptide [4Fe-4S] cluster (FX) as an intermediate electron acceptor and two [4Fe-4S] iron-sulfur clusters (FA and FB) as the terminal electron acceptors. This article focuses on type I reaction centers with special attention paid to the spectroscopic properties of FX, FA, and FB, and to the biochemical properties of the polypeptides that bind these iron-sulfur clusters.
| Original language | English (US) |
|---|---|
| Title of host publication | Encyclopedia of Biological Chemistry |
| Subtitle of host publication | Second Edition |
| Publisher | Elsevier Inc. |
| Pages | 335-342 |
| Number of pages | 8 |
| ISBN (Electronic) | 9780123786319 |
| ISBN (Print) | 9780123786302 |
| DOIs | |
| State | Published - Feb 15 2013 |
All Science Journal Classification (ASJC) codes
- General Biochemistry, Genetics and Molecular Biology
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