May 4, 2006

Structure and function of photosystems I and II

Annual Review of Plant Biology
Nathan Nelson, C F Yocum

Abstract

Oxygenic photosynthesis, the principal converter of sunlight into chemical energy on earth, is catalyzed by four multi-subunit membrane-protein complexes: photosystem I (PSI), photosystem II (PSII), the cytochrome b(6)f complex, and F-ATPase. PSI generates the most negative redox potential in nature and largely determines the global amount of enthalpy in living systems. PSII generates an oxidant whose redox potential is high enough to enable it to oxidize H(2)O, a substrate so abundant that it assures a practically unlimited electron source for life on earth. During the last century, the sophisticated techniques of spectroscopy, molecular genetics, and biochemistry were used to reveal the structure and function of the two photosystems. The new structures of PSI and PSII from cyanobacteria, algae, and plants has shed light not only on the architecture and mechanism of action of these intricate membrane complexes, but also on the evolutionary forces that shaped oxygenic photosynthesis.

  • References256
  • Citations285

Mentioned in this Paper

Adenosine Triphosphatases
Complex (molecular entity)
Oxidation
Protein Conformation
Oxidation-Reduction
Spectrum Analysis
Photosystem I
Algae
Drug Kinetics
Adenosinetriphosphatase

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