Time-Resolved Vibrational Analysis of Quinone Binding and Interaction in the Electron Transfer of Bacterial Photosynthetic Reaction Centers View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1992

AUTHORS

R. Hienerwadel , D. Thibodeau , F. Lenz , J. Breton , E. Nabedryk , W. Kreutz , W. Mäntele

ABSTRACT

The understanding of the sequence of events, the mechanisms of reactions and the identity of reaction partners in the primary electron transfer of photosynthesis mainly arises from time-resolved spectroscopic techniques (for a review, see [1]). These primary steps of energy conversion take place in reaction centers (RC) which contain well-organized pigments and redox components. In purple photosynthetic bacteria, electron transport upon photoexcitation proceeds within 2–3 picoseconds from the primary electron donor “P” (a BChl2) to the monomelic BPheo “H” and from H to the primary acceptor quinone within approx. 200 psec. In the presence of the secondary quinone QA, electron transfer from QA to QB proceeds within approx. 150 μsec. QA and QB are the first electron acceptors stable in the msec-to-second range. If the redox energy stored in the P+QB− state is not used by secondary redox reactions, charge recombination with a half-time of 0.5-1 sec observed In the absence of QB, charge recombination from QA proceeds within ca. 70 msec. More... »

PAGES

83-86

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-84771-4_25

DOI

http://dx.doi.org/10.1007/978-3-642-84771-4_25

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041123954


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