Crystallization of photosystem II for time-resolved structural studies using an X-ray free electron laser

Jesse Coe, Christopher Kupitz, Shibom Basu, Chelsie E. Conrad, Shatabdi Roy-Chowdhury, Raimund Fromme, Petra Fromme

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)

Abstract

Photosystem II (PSII) is a membrane protein supercomplex that executes the initial reaction of photosynthesis in higher plants, algae, and cyanobacteria. It captures the light from the sun to catalyze a transmembrane charge separation. In a series of four charge separation events, utilizing the energy from four photons, PSII oxidizes two water molecules to obtain dioxygen, four protons, and four electrons. The light reactions of photosystems I and II (PSI and PSII) result in the formation of an electrochemical transmembrane proton gradient that is used for the production of ATP. Electrons that are subsequently transferred from PSI via the soluble protein ferredoxin to ferredoxin-NADP+ reductase that reduces NADP+ to NADPH. The products of photosynthesis and the elemental oxygen evolved sustain all higher life on Earth. All oxygen in the atmosphere is produced by the oxygen-evolving complex in PSII, a process that changed our planet from an anoxygenic to an oxygenic atmosphere 2.5 billion years ago. In this chapter, we provide recent insight into the mechanisms of this process and methods used in probing this question.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc
Pages459-482
Number of pages24
DOIs
Publication statusPublished - Jan 1 2015

Publication series

NameMethods in Enzymology
Volume557
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Coe, J., Kupitz, C., Basu, S., Conrad, C. E., Roy-Chowdhury, S., Fromme, R., & Fromme, P. (2015). Crystallization of photosystem II for time-resolved structural studies using an X-ray free electron laser. In Methods in Enzymology (pp. 459-482). (Methods in Enzymology; Vol. 557). Academic Press Inc. https://doi.org/10.1016/bs.mie.2015.01.011