Protein/lipid interaction in the bacterial photosynthetic reaction center: Phosphatidylcholine and phosphatidylglycerol modify the free energy levels of the quinones

László Nagy, Francesco Milano, Márta Dorogi, Angela Agostiano, Gábor Laczkó, Kornélia Szebényi, G. Váró, Massimo Trotta, P. Maróti

Research output: Contribution to journalArticle

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Abstract

The role of characteristic phospholipids of native membranes, phosphatidylcholine (PC), phosphatidylglycerol (PG), and cardiolipin (CL), was studied in the energetics of the acceptor quinone side in photosynthetic reaction centers of Rhodobacter sphaeroides. The rates of the first, k AB(1), and the second, kAB(2), electron transfer and that of the charge recombination, kBP, the free energy levels of Q A-QB and QAQB- states, and the changes of charge compensating protein relaxation were determined in RCs incorporated into artificial lipid bilayer membranes. In RCs embedded in the PC vesicle, kAB(1) and kAB(2) increased (from 3100 to 4100 s-1 and from 740 to 3300 s-1, respectively) and kBP decreased (from 0.77 to 0.39 s-1) compared to those measured in detergent at pH 7. In PG, kAB(1) and kBP decreased (to values of 710 and 0.26 s-1, respectively), while kAB(2) increased to 1506 s-1 at pH 7. The free energy between the QA-QB and Q AQB- states decreased in PC and PG (ΔG°QA-QB→QAQ B- = -76.9 and -88.5 meV, respectively) compared to that measured in detergent (-61.8 meV). The changes of the QA/Q A- redox potential measured by delayed luminescence showed (1) a differential effect of lipids whether RC incorporated in micelles or vesicles, (2) an altered binding interaction between anionic lipids and RC, (3) a direct influence of PC and PG on the free energy levels of the primary and secondary quinones probably through the intraprotein hydrogen-bonding network, and (4) a larger increase of the QA/QA- free energy in PG than in PC both in detergent micelles and in single-component vesicles. On the basis of recent structural data, implications of the binding properties of phospholipids to RC and possible interactions between lipids and electron transfer components will be discussed.

Original languageEnglish
Pages (from-to)12913-12923
Number of pages11
JournalBiochemistry
Volume43
Issue number40
DOIs
Publication statusPublished - Oct 12 2004

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Photosynthetic Reaction Center Complex Proteins
Quinones
Phosphatidylglycerols
Phosphatidylcholines
Electron energy levels
Free energy
Lipids
Detergents
Micelles
Proteins
Phospholipids
Electrons
Rhodobacter sphaeroides
Cardiolipins
Lipid bilayers
Membranes
Lipid Bilayers
Hydrogen Bonding
Membrane Lipids
Luminescence

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein/lipid interaction in the bacterial photosynthetic reaction center : Phosphatidylcholine and phosphatidylglycerol modify the free energy levels of the quinones. / Nagy, László; Milano, Francesco; Dorogi, Márta; Agostiano, Angela; Laczkó, Gábor; Szebényi, Kornélia; Váró, G.; Trotta, Massimo; Maróti, P.

In: Biochemistry, Vol. 43, No. 40, 12.10.2004, p. 12913-12923.

Research output: Contribution to journalArticle

Nagy, László ; Milano, Francesco ; Dorogi, Márta ; Agostiano, Angela ; Laczkó, Gábor ; Szebényi, Kornélia ; Váró, G. ; Trotta, Massimo ; Maróti, P. / Protein/lipid interaction in the bacterial photosynthetic reaction center : Phosphatidylcholine and phosphatidylglycerol modify the free energy levels of the quinones. In: Biochemistry. 2004 ; Vol. 43, No. 40. pp. 12913-12923.
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AU - Agostiano, Angela

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AU - Szebényi, Kornélia

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