Keyword search (4,163 papers available)

"Kalman L" 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 Bound detergent molecules in bacterial reaction centers facilitate detection of tetryl explosive. Modafferi D, Zazubovich V, Kálmán L 32632533
PHYSICS
4 Proton release due to manganese binding and oxidation in modified bacterial reaction centers. Kálmán L, Thielges MC, Williams JC, Allen JP 16201752
PHYSICS
5 Comparison of bacterial reaction centers and photosystem II. Kálmán L, Williams JC, Allen JP 18853275
PHYSICS
6 Effect of anions on the binding and oxidation of divalent manganese and iron in modified bacterial reaction centers. Tang K, Williams JC, Allen JP, Kálmán L 19383473
PHYSICS
7 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
8 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
9 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
10 Lipid binding to the carotenoid binding site in photosynthetic reaction centers. Deshmukh SS, Tang K, Kálmán L 21894992
PHYSICS
11 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
12 Low potential manganese ions as efficient electron donors in native anoxygenic bacteria. Deshmukh SS, Protheroe C, Ivanescu MA, Lag S, Kálmán L 29355486
PHYSICS

 

Title:Photoactivation and conformational gating for manganese binding and oxidation in bacterial reaction centers
Authors:Samaei ADeshmukh SSProtheroe CNyéki STremblay-Ethier RAKálmán L
Link:https://pubmed.ncbi.nlm.nih.gov/36216075/
DOI:10.1016/j.bbabio.2022.148928
Publication:Biochimica et biophysica acta. Bioenergetics
Keywords:Electron transferEnergy conversionMetal bindingPhotosynthesisStructural change
PMID:36216075 Category: Date Added:2022-10-11
Dept Affiliation: PHYSICS
1 Department of Physics, Concordia University, Montreal, QC, Canada.
2 Department of Physics, Concordia University, Montreal, QC, Canada. Electronic address: laszlo.kalman@concordia.ca.

Description:

The influence of illumination history of native bacterial reaction centers (BRCs) on the ability of binding and photo-induced oxidation of manganous ions was investigated in the pH range between 8.0 and 9.4. Binding of manganous ions to a buried site required 6 to 11-fold longer incubation periods, depending on the pH, in dark-adapted BRCs than in BRCs that were previously illuminated prior to manganese binding. The intrinsic electron transfer from the bound manganese ion to the photo-oxidized primary electron donor was found to be limited by a 2 to 5-fold slower precursor conformational step in the dark-adapted samples for the same pH range. The conformational gating could be eliminated by photoactivation, namely if the BRCs were illuminated prior to binding. Unlike in Photosystem II, photoactivation in BRCs did not involve cluster assembly. Photoactivation with manganese already bound was only possible at elevated detergent concentration. In addition, also exclusively in dark-adapted BRCs, a marked breaking point in the Arrhenius-plot was discovered around 15 °C at pH 9.4 indicating a change in the reaction mechanism, most likely caused by the change of orientation of the 2-acetyl group of the inactive bacteriochlorophyll monomer located near the manganese binding site.





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