Light-induced structural changes and the site of O=O bond formation in PSII caught by XFEL

Journal: Nature

Published: 2017-03-01

DOI: 10.1038/nature21400

Affiliations: 14

Authors: 38

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Research Highlight

Seeing the light reaction

© Yasuhide Fumoto/Digital Vision/Getty

© Yasuhide Fumoto/Digital Vision/Getty

Fast electron laser pulses are helping unravel the precise mechanism by which plants capture energy from sunlight.

Okayama University researchers co-led a study of Photosystem II, the vast protein that handles the photosynthetic step in which light drives the oxidation of water to release molecular oxygen.

The team analyzed the protein using X-ray free electron lasers (XFEL), firing a powerful femtosecond — just one quadrillionth of a second — pulse of electrons at the protein. The electrons bounce off the atoms in the protein; by measuring the electron scatter pattern, the team can work backward to calculate where all the protein’s atoms are, revealing its structure.

Using flashes of light to simulate sunlight, followed by precisely timed XFEL pulses, the researchers captured before-and-after images of the protein during oxygen formation. Comparing the two images, they identified the key atomic motions within the protein as the oxygen molecule was formed, pinpointing the probable spot where the molecule is made.

Supported content

  1. Nature 543, 131– 135 (2017). doi: 10.1038/nature21400
Institutions FC WFC
RIKEN SPring-8 Center (RSC), Japan 0.38 0.38
Research Institute for Interdisciplinary Science (RIIS), Okayama University, Japan 0.16 0.16
Graduate School of Natural Science and Technology, Okayama University, Japan 0.16 0.16
Japan Synchrotron Radiation Research Institute (JASRI), Japan 0.09 0.09
Department of Biological Sciences, UTokyo, Japan 0.05 0.05
Division of Material Science, Nagoya University, Japan 0.05 0.05
Department of Cell Biology, Kyoto University, Japan 0.03 0.03
Picobiology Institute, University of Hyogo, Japan 0.02 0.02
CAS Key Laboratory of Photobiology, IBCAS CAS, China 0.02 0.02
Institute for Protein Research (IPR), Osaka University, Japan 0.01 0.01
Division of Food Science and Biotechnology, Kyoto University, Japan 0.01 0.01
Department of Cell Biology and Anatomy, UTokyo, Japan 0.01 0.01
Department of Chemistry, Kobe University, Japan 0.01 0.01

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