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|
|Number of pages||8|
|State||Published - Feb 15 2013|
All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)