Studies of Electron Transport Dynamics in Photosynthetic Reaction Centers Using Fast Temperature Changes

S. K. Chamorovsky^1*, P. P. Knox¹, B. V. Zubov², and I. V. Chizhov²

¹School of Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-1115; E-mail: serch@bioh.phys.msu.su; knox@biophys.msu.ru

²Institute of General Physics, Russian Academy of Sciences, Moscow, Russia; fax: (095) 132-6056; E-mail: zubov@nsc.gpi.ru

^* To whom correspondence should be addressed.

Received October 10, 2000; Revision received October 31, 2000

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Rates of thermoinduced conformational transitions of reaction center (RC) complexes providing effective electron transport were studied in chromatophores and isolated RC preparations of various photosynthesizing purple bacteria using methods of fast freezing and laser-induced temperature jump. Reactions of electron transfer from the primary to secondary quinone acceptors and from the multiheme cytochrome c subunit to photoactive bacteriochlorophyll dimer were used as probes of electron transport efficiency. The thermoinduced transition of the acceptor complex to the conformational state facilitating electron transfer to the secondary quinone acceptor was studied. It was shown that neither the characteristic time of the thermoinduced transition within the temperature range 233-253 K nor the characteristic time of spontaneous decay of this state at 253 K exceeded several tens of milliseconds. In contrast to the quinone complex, the thermoinduced transition of the macromolecular RC complex to the state providing effective electron transport from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer within the temperature range 220-280 K accounts for tens of seconds. This transition is thought to be mediated by large-scale conformational dynamics of the macromolecular RC complex.

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KEY WORDS: photosynthetic reaction center, cytochromes, electron transport, conformational changes, purple bacteria

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