Resonance Raman studies of the photosynthetic membrane proteins

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

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Citation (Scopus)

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)
Title of host publicationProceedings of SPIE - The International Society for Optical Engineering
EditorsSergei A. Akhmanov, Marina Yu. Poroshina
PublisherPubl by Int Soc for Optical Engineering
Pages59-65
Number of pages7
Volume1403
Editionpt 1
StatePublished - 1991
Externally publishedYes
EventInternational Conference on Laser Applications in Life Sciences - Moscow, USSR
Duration: Aug 27 1990Aug 31 1990

Other

OtherInternational Conference on Laser Applications in Life Sciences
CityMoscow, USSR
Period8/27/908/31/90

Fingerprint

Photosynthetic membranes
polarization (charge separation)
membranes
proteins
Proteins
tyrosine
mutations
pigments
Pigments
bacteria
Bacteria
Positive ions
Pumps
pumps
cations
Molecules
Electrons
probes
molecules
electrons

ASJC Scopus subject areas

  • Electrical and Electronic Engineering
  • Condensed Matter Physics

Cite this

Lutz, M., Mattioli, T., Moenne-Loccoz, P., Qing, Z., & Robert, B. (1991). Resonance Raman studies of the photosynthetic membrane proteins. In S. A. Akhmanov, & M. Y. Poroshina (Eds.), Proceedings of SPIE - The International Society for Optical Engineering (pt 1 ed., Vol. 1403, pp. 59-65). Publ by Int Soc for Optical Engineering.

Resonance Raman studies of the photosynthetic membrane proteins. / Lutz, Marc; Mattioli, Tony; Moenne-Loccoz, Pierre; Qing, Zhou; Robert, Bruno.

Proceedings of SPIE - The International Society for Optical Engineering. ed. / Sergei A. Akhmanov; Marina Yu. Poroshina. Vol. 1403 pt 1. ed. Publ by Int Soc for Optical Engineering, 1991. p. 59-65.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Lutz, M, Mattioli, T, Moenne-Loccoz, P, Qing, Z & Robert, B 1991, Resonance Raman studies of the photosynthetic membrane proteins. in SA Akhmanov & MY Poroshina (eds), Proceedings of SPIE - The International Society for Optical Engineering. pt 1 edn, vol. 1403, Publ by Int Soc for Optical Engineering, pp. 59-65, International Conference on Laser Applications in Life Sciences, Moscow, USSR, 8/27/90.
Lutz M, Mattioli T, Moenne-Loccoz P, Qing Z, Robert B. Resonance Raman studies of the photosynthetic membrane proteins. In Akhmanov SA, Poroshina MY, editors, Proceedings of SPIE - The International Society for Optical Engineering. pt 1 ed. Vol. 1403. Publ by Int Soc for Optical Engineering. 1991. p. 59-65
Lutz, Marc ; Mattioli, Tony ; Moenne-Loccoz, Pierre ; Qing, Zhou ; Robert, Bruno. / Resonance Raman studies of the photosynthetic membrane proteins. Proceedings of SPIE - The International Society for Optical Engineering. editor / Sergei A. Akhmanov ; Marina Yu. Poroshina. Vol. 1403 pt 1. ed. Publ by Int Soc for Optical Engineering, 1991. pp. 59-65
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AB - 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.

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