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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:The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.
Authors:Balhara V,  Deshmukh SS,  Kálmán L,  Kornblatt JA
Link:https://www.ncbi.nlm.nih.gov/pubmed/24520380?dopt=Abstract
Category:PLoS One
PMID:24520380
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montréal, Quebec, Canada.
2 Department of Physics, Concordia University, Montréal, Quebec, Canada.
3 Department of Biology and the Centre for Structural and Functional Genomics, Concordia University, Montréal, Quebec, Canada.

Description:

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

PLoS One. 2014;9(2):e88395

Authors: Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

Abstract

The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in which the two proteins would bind to one another. The two native proteins in solution would not bind under any of the tried conditions. We found that if the structures were perturbed binding would occur. We stated that only the non-native Str enolase or Pgn would interact such that we could detect binding. We report here the results of a series of dual polarization interferometry (DPI) experiments coupled with atomic force microscopy (AFM), isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence. We show that the critical condition for forming stable complexes of the two native proteins involves Str enolase binding to a surface. Surfaces that attract Str enolase are a sufficient condition for binding Pgn. Under certain conditions, Pgn adsorbed to a surface will bind Str enolase.

PMID: 24520380 [PubMed - indexed for MEDLINE]