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Updated: Aug 12, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Interactions between the donor and acceptor sides in bacterial reaction centers
1CEA-DEVM/LBC, Cadarache, 13108 Saint Paul-lez Durance, France.
The equilibrium constant for electron transfer between quinone acceptors in Rhodobacter capsulatus reaction centers differs significantly depending on the redox state of the primary donor P. This difference is linked to conformational changes influenced by ubiquinone or inhibitor binding at the Q(B) site.
Area of Science:
- Photosynthesis research
- Biochemistry
- Electron transport chains
Background:
- The reaction center of Rhodobacter capsulatus facilitates crucial electron transfer processes.
- Understanding quinone acceptor interactions is key to photosynthesis research.
Purpose of the Study:
- To measure the apparent equilibrium constant K'(2) for electron transfer between primary (Q(A)) and secondary (Q(B)) quinone acceptors.
- To investigate the influence of the primary donor's redox state (P(+) or P) on this equilibrium.
- To explore the impact of ubiquinone and inhibitor binding on donor-acceptor interactions.
Main Methods:
- Measurement of K'(2) in chromatophores of Rhodobacter capsulatus.
- Utilizing recombination rates from P(+)Q(A-) and P(+)Q(B-) states.
- Analyzing semiquinone oscillations during single turnover flashes.
- Measuring midpoint potential shifts of P in the presence of Q(B-) or Q(A-)S (stigmatellin).
Main Results:
- K'(2)(P(+)) was approximately 100, while K'(2)(P) was approximately 20, indicating a 5-fold difference.
- Stabilization of the oxidized primary donor P(+) by 10 mV (with Q(B-)) and 30 mV (with Q(A-)S).
- Observed modifications in P(+)/P and Q(A)/Q(A)(-) interactions based on Q(B) pocket occupancy.
Conclusions:
- The occupancy of the Q(B) pocket by ubiquinone or stigmatellin significantly alters interactions between the primary donor and quinone acceptors.
- A proposed conformational destabilization of the P(+)Q(A-) state contributes to the high K'(2)(P(+)) value, which is relieved by stigmatellin binding.
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