Journal
SCIENCE
Volume 357, Issue 6355, Pages 1021-1025Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan5611
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Funding
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences, of the U.S. Department of Energy (DOE) [DE-SC0010575]
- National Institutes of Health
- National Institute of General Medical Sciences
- Howard Hughes Medical Institute
- DOE Office of Science, Office of Biological and Environmental Research
- 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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