FX, FA, and FB Iron-Sulfur Clusters in Type I Photosynthetic Reaction Centers

B. Jagannathan, J. H. Golbeck

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


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 languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Number of pages8
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
StatePublished - Feb 15 2013

All Science Journal Classification (ASJC) codes

  • General Biochemistry, Genetics and Molecular Biology


Dive into the research topics of 'FX, FA, and FB Iron-Sulfur Clusters in Type I Photosynthetic Reaction Centers'. Together they form a unique fingerprint.

Cite this