Pulsed EPR structure analysis of photosystem I single crystals: Localization of the phylloquinone acceptor

Robert Bittl, Stephan G. Zech, Petra Fromme, Horst T. Witt, Wolfgang Lubitz

Research output: Contribution to journalArticle

70 Scopus citations

Abstract

A novel application of electron paramagnetic resonance (EPR) is reported to gain three dimensional structural information on cofactors in proteins. The method is applied here to determine the unknown position of the electron acceptor Q(K), a phylloquinone (vitamin K1), in the electron transfer chain in photosystem I of oxygenic photosynthesis. The unusual electron spin echo (out-of-phase echo) observed for the light induced radical pair P700/(·+)Q(K)/(·-) in PS I allows the measurement of the dipolar coupling between the two radical pair spins which yields directly the distance between these two radicals. Full advantage of the information in the out-of-phase echo modulation can be taken if measurements using single crystals are performed. With such samples, the orientation of the principal axis of the dipolar interaction, i.e., the axis connecting P700/(·+) and Q(K)/(·-), can be determined with respect to the crystal axes system. An angle of Θ = (27 ±5)°between the dipolar coupling axis and the crystallographic c-axis has been derived from the modulation of the out-of- phase echo. Furthermore, the projection of the dipolar axis onto the crystallographic a,b-plane, is found to be parallel to the a-axis. The results allow for the determination of two possible locations of Q(K) within the electron transfer chain of photosystem I. These two positions are related to each other by the pseudo C2 symmetry of the chlorophyll cofactors.

Original languageEnglish (US)
Pages (from-to)12001-12004
Number of pages4
JournalBiochemistry
Volume36
Issue number40
DOIs
StatePublished - Oct 7 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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