Keyword search (4,163 papers available)

"Deshmukh SS" Authored Publications:

Title Authors PubMed ID
1 Photoactivation and conformational gating for manganese binding and oxidation in bacterial reaction centers Samaei A; Deshmukh SS; Protheroe C; Nyéki S; Tremblay-Ethier RA; Kálmán L; 36216075
PHYSICS
2 Tuning the redox potential of the primary electron donor in bacterial reaction centers by manganese binding and light-induced structural changes. Deshmukh SS, Kálmán L 32777306
PHYSICS
3 Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer. Deshmukh SS, Williams JC, Allen JP, Kálmán L 21141811
PHYSICS
4 Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer. Deshmukh SS, Williams JC, Allen JP, Kálmán L 21410139
PHYSICS
5 Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor. Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L 21561160
PHYSICS
6 Lipid binding to the carotenoid binding site in photosynthetic reaction centers. Deshmukh SS, Tang K, Kálmán L 21894992
PHYSICS
7 The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation. Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA 24520380
CHEMBIOCHEM
8 Low potential manganese ions as efficient electron donors in native anoxygenic bacteria. Deshmukh SS, Protheroe C, Ivanescu MA, Lag S, Kálmán L 29355486
PHYSICS
9 The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen. Deshmukh SS, Kornblatt MJ, Kornblatt JA 30653526
BIOLOGY

 

Title:Lipid binding to the carotenoid binding site in photosynthetic reaction centers.
Authors:Deshmukh SSTang KKálmán L
Link:https://www.ncbi.nlm.nih.gov/pubmed/21894992?dopt=Abstract
Publication:
Keywords:
PMID:21894992 Category:J Am Chem Soc Date Added:2019-06-04
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]





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