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Tuning the redox potential of the primary electron donor in bacterial reaction centers by manganese binding and light-induced structural changes.

Author(s): Deshmukh SS, Kálmán L

Biochim Biophys Acta Bioenerg. 2020 Aug 07;:148285 Authors: Deshmukh SS, Kálmán L

Article GUID: 32777306

Bound detergent molecules in bacterial reaction centers facilitate detection of tetryl explosive.

Author(s): Modafferi D, Zazubovich V, Kálmán L

Photosynth Res. 2020 Jul 06;: Authors: Modafferi D, Zazubovich V, Kálmán L

Article GUID: 32632533

Proton release due to manganese binding and oxidation in modified bacterial reaction centers.

Author(s): Kálmán L, Thielges MC, Williams JC, Allen JP

Biochemistry. 2005 Oct 11;44(40):13266-73 Authors: Kálmán L, Thielges MC, Williams JC, Allen JP

Article GUID: 16201752

Comparison of bacterial reaction centers and photosystem II.

Author(s): Kálmán L, Williams JC, Allen JP

Photosynth Res. 2008 Oct-Dec;98(1-3):643-55 Authors: Kálmán L, Williams JC, Allen JP

Article GUID: 18853275

Effect of anions on the binding and oxidation of divalent manganese and iron in modified bacterial reaction centers.

Author(s): Tang K, Williams JC, Allen JP, Kálmán L

Biophys J. 2009 Apr 22;96(8):3295-304 Authors: Tang K, Williams JC, Allen JP, Kálmán L

Article GUID: 19383473

Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer.

Author(s): Deshmukh SS, Williams JC, Allen JP, Kálmán L

Biochemistry. 2011 Jan 25;50(3):340-8 Authors: Deshmukh SS, Williams JC, Allen JP, Kálmán L

Article GUID: 21141811

Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer.

Author(s): Deshmukh SS, Williams JC, Allen JP, Kálmán L

Biochemistry. 2011 Apr 26;50(16):3321-31 Authors: Deshmukh SS, Williams JC, Allen JP, Kálmán L

Article GUID: 21410139

Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor.

Author(s): Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L

Biochemistry. 2011 Jun 14;50(23):5249-62 Authors: Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L

Article GUID: 21561160

Lipid binding to the carotenoid binding site in photosynthetic reaction centers.

Author(s): Deshmukh SS, Tang K, Kálmán L

J Am Chem Soc. 2011 Oct 12;133(40):16309-16 Authors: Deshmukh SS, Tang K, Kálmán L

Article GUID: 21894992

The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.

Author(s): Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

PLoS One. 2014;9(2):e88395 Authors: Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

Article GUID: 24520380

Low potential manganese ions as efficient electron donors in native anoxygenic bacteria.

Author(s): Deshmukh SS, Protheroe C, Ivanescu MA, Lag S, Kálmán L

Biochim Biophys Acta Bioenerg. 2018 Apr;1859(4):227-233 Authors: Deshmukh SS, Protheroe C, Ivanescu MA, Lag S, Kálmán L

Article GUID: 29355486


Title:Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer.
Authors:Deshmukh SSWilliams JCAllen JPKálmán L
Link:https://www.ncbi.nlm.nih.gov/pubmed/21141811?dopt=Abstract
Category:Biochemistry
PMID:21141811
Dept Affiliation: PHYSICS
1 Department of Physics, Concordia University, Montreal, Quebec H4B 1R6, Canada.

Description:

Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer.

Biochemistry. 2011 Jan 25;50(3):340-8

Authors: Deshmukh SS, Williams JC, Allen JP, Kálmán L

Abstract

Conformational changes near the bacteriochlorophyll dimer induced by continuous illumination were identified in the wild type and 11 different mutants of reaction centers from Rhodobacter sphaeroides. The properties of the bacteriochlorophyll dimer, which has a different hydrogen bonding pattern with the surrounding protein in each mutant, were characterized by steady-state and transient optical spectroscopy. After illumination for 1 min, in the absence of the secondary quinone, the recovery of the charge-separated states was nearly 1 order of magnitude slower in one group of mutants including the wild type than in the mutants carrying the Leu to His mutation at the L131 position. The slower recovery was accompanied by a substantial decrease in the electrochromic absorption changes associated with the Q(y) bands of the nearby monomers during the illumination. The other set of mutants containing the Leu L131 to His substitution exhibited slightly altered electrochromic changes that decreased only half as much during the illumination as in the other family of mutants. The correlation between the recovery of the charge-separated states in the light-induced conformation and the electrochromic absorption changes suggests a dielectric relaxation of the protein that stabilizes the charge on the dimer.

PMID: 21141811 [PubMed - indexed for MEDLINE]