Evidence map›Paper›PMID 25606686›Full record

ArticleBiophysical journal2015

Stigmatellin probes the electrostatic potential in the QB site of the photosynthetic reaction center.

László Gerencsér, Bogáta Boros, Valerie Derrien, Deborah K Hanson, Colin A Wraight, Pierre Sebban, Péter Maróti

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Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

László GerencsérDepartment of Biophysics, University of Szeged, Szeged, Hungary; Department of Physics and Astronomy, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands. Electronic address: l.gerencser@vu.nl.
Bogáta BorosDepartment of Biophysics, University of Szeged, Szeged, Hungary.
Valerie DerrienLaboratoire de Chimie Physique, University of Paris-Sud, Orsay, France.
Deborah K HansonBiosciences Divisions, Argonne National Laboratory, Argonne, Illinois.
Colin A WraightDepartment of Biochemistry and Center for Biophysics and Computational Biology, University of Illinois, Urbana, Illinois.
Pierre SebbanLaboratoire de Chimie Physique, University of Paris-Sud, Orsay, France.
Péter MarótiDepartment of Biophysics, University of Szeged, Szeged, Hungary. Electronic address: pmaroti@sol.cc.u-szeged.hu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The electrostatic potential in the secondary quinone (QB) binding site of the reaction center (RC) of the photosynthetic bacterium Rhodobacter sphaeroides determines the rate and free energy change (driving force) of electron transfer to QB. It is controlled by the ionization states of residues in a strongly interacting cluster around the QB site. Reduction of the QB induces change of the ionization states of residues and binding of protons from the bulk. Stigmatellin, an inhibitor of the mitochondrial and photosynthetic respiratory chain, has been proven to be a unique voltage probe of the QB binding pocket. It binds to the QB site with high affinity, and the pK value of its phenolic group monitors the local electrostatic potential with high sensitivity. Investigations with different types of detergent as a model system of isolated RC revealed that the pK of stigmatellin was controlled overwhelmingly by electrostatic and slightly by hydrophobic interactions. Measurements showed a high pK value (>11) of stigmatellin in the QB pocket of the dark-state wild-type RC, indicating substantial negative potential. When the local electrostatics of the QB site was modulated by a single mutation, L213Asp → Ala, or double mutations, L213Asp-L212Glu → Ala-Ala (AA), the pK of stigmatellin dropped to 7.5 and 7.4, respectively, which corresponds to a >210 mV increase in the electrostatic potential relative to the wild-type RC. This significant pK drop (ΔpK > 3.5) decreased dramatically to (ΔpK > 0.75) in the RC of the compensatory mutant (AA+M44Asn → AA+M44Asp). Our results indicate that the L213Asp is the most important actor in the control of the electrostatic potential in the QB site of the dark-state wild-type RC, in good accordance with conclusions of former studies using theoretical calculations or light-induced charge recombination assay.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsBenzoquinonesBinding SitesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsPolyenesProtein BindingRhodobacter sphaeroidesStatic ElectricityAnti-Bacterial AgentsBenzoquinonesPhotosynthetic Reaction Center Complex ProteinsPolyenesquinonestigmatellin

Identifiers

PMID25606686
PMCPMC4302209

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.