Resonance Raman studies of the photosynthetic membrane proteins

Marc Lutz, Tony Mattioli, Pierre Moenne-Loccoz, Zhou Qing, Bruno Robert

Research output: Contribution to journalConference article

2 Scopus citations

Abstract

Examples of recent resonance Raman (RR) studies conducted on reaction center (RC) proteins of photosynthetic bacteria and plants are given. These include structural studies of the primary donors of bacterial and Photosystem 1 RCs as well as of the early electron acceptors of bacterial and Photosystem 2 RCs. Pump-probe, steady state, difference RR experiments, and time-resolved RR studies of the 12 ns-lived P+H-Q- state conducted on RCs of the R26 mutant of Rhb sphaeroides, showed that a long-lived, triggered protein conformational change occurs on a nanosecond timescale around the functional, L-side bacteriochlorophyll a (BChl) molecule in bacterial RCs, upon formation of the P+ radical cation state. The origin of the influence of the M210 tyrosine side-chain on the primary charge separation has been investigated on two site-directed mutants. The mutations did not significantly alter the local interactions of any of the L-side pigments, hence indicating that Tyr M208 must act directly on intermediate states of the charge separation.

Original languageEnglish (US)
Pages (from-to)59-65
Number of pages7
JournalProceedings of SPIE - The International Society for Optical Engineering
Volume1403
Issue numberpt 1
StatePublished - Jan 1 1991
EventInternational Conference on Laser Applications in Life Sciences - Moscow, USSR
Duration: Aug 27 1990Aug 31 1990

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Computer Science Applications
  • Applied Mathematics
  • Electrical and Electronic Engineering

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