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Structure of a symmetric photosynthetic reaction center-photosystem.

Christopher J GisrielIosifina SarrouBryan H FerlezJohn H GolbeckKevin E ReddingRaimund Fromme
Published in: Science (New York, N.Y.) (2017)
Reaction centers are pigment-protein complexes that drive photosynthesis by converting light into chemical energy. It is believed that they arose once from a homodimeric protein. The symmetry of a homodimer is broken in heterodimeric reaction-center structures, such as those reported previously. The 2.2-angstrom resolution x-ray structure of the homodimeric reaction center-photosystem from the phototroph Heliobacterium modesticaldum exhibits perfect C2 symmetry. The core polypeptide dimer and two small subunits coordinate 54 bacteriochlorophylls and 2 carotenoids that capture and transfer energy to the electron transfer chain at the center, which performs charge separation and consists of 6 (bacterio)chlorophylls and an iron-sulfur cluster; unlike other reaction centers, it lacks a bound quinone. This structure preserves characteristics of the ancestral reaction center, providing insight into the evolution of photosynthesis.
Keyphrases
  • electron transfer
  • high resolution
  • magnetic resonance imaging
  • computed tomography
  • protein protein
  • mass spectrometry
  • small molecule
  • contrast enhanced