4.8 Article

Structure of a symmetric photosynthetic reaction center-photosystem

Journal

SCIENCE
Volume 357, Issue 6355, Pages 1021-1025

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan5611

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Funding

  1. Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences, of the U.S. Department of Energy (DOE) [DE-SC0010575]
  2. National Institutes of Health
  3. National Institute of General Medical Sciences
  4. Howard Hughes Medical Institute
  5. DOE Office of Science, Office of Biological and Environmental Research
  6. DOE Office of Science [DE-AC02-06CH11357]

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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 C-2 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.

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