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Turnover of ubiquinone-0 at the acceptor side of photosynthetic reaction center

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Abstract

The steady-state operation of photosynthetic reaction center from Rhodobacter sphaeroides was investigated by measuring the rate of cytochrome photo-oxidation under intensive continuous illumination (808 nm, 5 W cm−2). The native quinone UQ10 in QB binding site of the reaction center was substituted by tailless UQ0 and the binding parameters and the turnover rate of the UQ0 was studied to test the recently discovered light-intensity dependent acceptor side effect (Gerencsér and Maróti 2006). The binding parameters of UQ0 (k on = 2.1 × 105 M−1 s−1 and k off = 100 s−1) were characteristic to the RC exposed to high light-intensity. The dissociation constant (K D = 480 μM) determined under high light intensity is 2–3 times larger than that determined from flash-experiments. The light-intensity dependent acceleration of cytochrome turnover measured on reaction center of inhibited proton binding was independent of the type of the quinone and was sensitive only to the size (“pressure”) of the quinone pool. The dissociation constants of different types of semiquinones show similarly high (several orders of magnitude) increase in the modified conformation of the QB binding pocket due to high intensity of illumination. This result indicates the exclusive role of the quinone headgroup in the binding of semiquinone to different conformations of the protein.

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Abbreviations

DEAE:

Diethylaminoethyl

DMBQ:

2,5-Dimethyl-1,4-benzoquinone

EDTA:

Ethylenediaminetetraacetic acid

LDAO:

N,N′-Dimethyl dodecylamine N-oxide

NHE:

Normal hydrogen electrode

P (P+):

Reduced (oxidized) bacteriochlorophyll dimer

QA and QB :

Primary and secondary quinone, respectively

RC:

Reaction center protein

SOD:

Superoxide dismutase

TMPD:

N,N,N′,N′-Tetramethyl-1,4-phenylenediamine

Triton X-100:

Polyoxyethylene(10) isooctylphenyl ether

UQ n :

2,3-Dimethoxy-5-methyl-1,4-benzoquinone with n isoprenoid units in the tail

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Acknowledgment

This work was financially supported by grants of NKTH-OTKA (K-67850) and Balaton (F-4/04). L.G. is indebted to Hungarian Academy of Sciences for Bolyai fellowship.

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Authors and Affiliations

  1. Department of Biophysics, University of Szeged, Egyetem utca 2, Szeged, 6722, Hungary

    László Gerencsér & Péter Maróti

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  1. László Gerencsér
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  2. Péter Maróti
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Correspondence to László Gerencsér.

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Regional Biophysics Conference of the National Biophysical Societies of Austria, Croatia, Hungary, Italy, Serbia, and Slovenia.

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Gerencsér, L., Maróti, P. Turnover of ubiquinone-0 at the acceptor side of photosynthetic reaction center. Eur Biophys J 37, 1195–1205 (2008). https://doi.org/10.1007/s00249-008-0290-3

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  • DOI: https://doi.org/10.1007/s00249-008-0290-3

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