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Studies on the electron transfer from Tyr-161 of polypeptide D-1 to P680+ in PS II membrane fragments from spinach

  • Chloroplasts
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Abstract

The functional connection between redox component Y z identified as Tyr-161 of polypeptide D-1 (Debus et al. 1988) and P680+ was analyzed by measurements of laser flash induced absorption changes at 830 nm in PS II membrane fragments from spinach. It was found that neither DCMU nor the ADRY agent 2-(3-chloro-4-trifluoromethyl) anilino-3,5-dinitrothiophene (ANT 2p) affects the rate of P680+ reduction by Y z under conditions where the catalytic site of water oxidation stays in the redox state S1. In contrast to that, a drastic retardation is observed after mild trypsin treatment at pH=6.0. This effect which is stimualted by flash illumination can be largely reversed by Ca2+. The above mentioned data lead to the following conclusions: (a) the segment of polypeptide D-1 containing Tyr-161 and coordination sites of P680 is not allosterically affected by structural changes due to DCMU binding at the QB-site which is also located in D-1. (b) ANT 2p as a strong protonophoric uncoupler and ADRY agent does not modify the reaction coordinate of P680+ reduction by Y z , and (c) Ca2+ could play a functional role for the electronic and vibrational coupling between the redox groups Y z and P680. The electron transport from Y z to P680+ is discussed within the framework of a nonadiabatic process. Based on thermodynamic considerations the reorganization energy is estimated to be in the order of 0.5 V.

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Abbreviations

ADRY:

acceleration of the deactivation reactions of the water splitting enzyme system Y

ANT 2p:

2-(3-chloro-4-trifluoromethyl)anilino-3,5 dinitrothiophene

DCMU:

3-(3,4-dichlorophenyl)-1,1-dimethylurea

MES:

2[N-Morpholino]ethanesulfonic acid

PS II:

photosystem II

QA, QB :

primary and secondary plastoquinone acceptor of photosystem II

S i :

redox states of the catalytic site of water oxidation

Y z :

redox active Tyr-161 of polypeptide D-1

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Authors and Affiliations

  1. Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität Berlin, Straßbe des 17. Juni 135, D 1000, Berlin 12, F.R.G.

    G. Renger, H-J. Eckert & M. Völker

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  1. G. Renger
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  2. H-J. Eckert
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  3. M. Völker
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Renger, G., Eckert, HJ. & Völker, M. Studies on the electron transfer from Tyr-161 of polypeptide D-1 to P680+ in PS II membrane fragments from spinach. Photosynth Res 22, 247–256 (1989). https://doi.org/10.1007/BF00048303

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  • DOI: https://doi.org/10.1007/BF00048303

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