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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
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
The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen.

Author(s): Deshmukh SS, Kornblatt MJ, Kornblatt JA

PLoS One. 2019;14(1):e0206338 Authors: Deshmukh SS, Kornblatt MJ, Kornblatt JA

Article GUID: 30653526
Title:Lipid binding to the carotenoid binding site in photosynthetic reaction centers.
Authors:Deshmukh SS,  Tang K,  Kálmán L
Link:https://www.ncbi.nlm.nih.gov/pubmed/21894992?dopt=Abstract
Category:J Am Chem Soc
PMID:21894992
Dept Affiliation: PHYSICS
1 Department of Physics, Concordia University, Montreal, Quebec H4B 1R6, Canada.

Description:

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

J Am Chem Soc. 2011 Oct 12;133(40):16309-16

Authors: Deshmukh SS, Tang K, Kálmán L

Abstract

Lipid binding to the carotenoid binding site near the inactive bacteriochlorophyll monomer was probed in the reaction centers of carotenoid-less mutant, R-26 from Rhodobacter sphaeroides. Recently, a marked light-induced change of the local dielectric constant in the vicinity of the inactive bacteriochlorophyll monomer was reported in wild type that was attributed to structural changes that ultimately lengthened the lifetime of the charge-separated state by 3 orders of magnitude (Deshmukh, S. S.; Williams, J. C.; Allen, J. P.; Kalman, L. Biochemistry 2011, 50, 340). Here in the R-26 reaction centers, the combination of light-induced structural changes and lipid binding resulted in a 5 orders of magnitude increase in the lifetime of the charge-separated state involving the oxidized dimer and the reduced primary quinone in proteoliposomes. Only saturated phospholipids with fatty acid chains of 12 and 14 carbon atoms long were bound successfully at 8 °C by cooling the reaction center protein slowly from room temperature. In addition to reporting a dramatic increase of the lifetime of the charge-separated state at physiologically relevant temperatures, this study reveals a novel lipid binding site in photosynthetic reaction center. These results shed light on a new potential application of the reaction center in energy storage as a light-driven biocapacitor since the charges separated by ~30 Å in a low-dielectric medium can be prevented from recombination for hours.

PMID: 21894992 [PubMed - indexed for MEDLINE]