Electronic Transitions of the Soret Band of Reaction Centers fromRhodobacter sphaeroidesStudied by Femtosecond Transient Absorbance Spectroscopy

2006 ◽  
Vol 110 (13) ◽  
pp. 6956-6961 ◽  
Author(s):  
Haiyu Wang ◽  
Su Lin ◽  
Neal W. Woodbury
Keyword(s):  
Soret Band ◽  
Reaction Centers ◽  
Electronic Transitions ◽  
Absorbance Spectroscopy ◽  
Transient Absorbance

scholarly journals Investigation of the Kinetics of Photoinduced Electronic Transitions in Nanostructures of Bacterial Reaction Centers

2016 ◽  
Vol 61 (10) ◽  
pp. 923-931
Author(s):  
Y.M. Barabash ◽  
◽  
M.A. Drapikovskyi ◽  
M.A. Zabolotny ◽  
M.P. Kulish ◽  
...  
Keyword(s):  
Reaction Centers ◽  
Electronic Transitions ◽  
Bacterial Reaction Centers ◽  
Kinetics Of

Time Resolution of Electronic Transitions of Photosynthetic Reaction Centers in the Infrared

1994 ◽  
Vol 98 (22) ◽  
pp. 5778-5783 ◽  
Author(s):  
G. C. Walker ◽  
S. Maiti ◽  
B. R. Cowen ◽  
C. C. Moser ◽  
P. L. Dutton ◽  
...  
Keyword(s):  
Time Resolution ◽  
Reaction Centers ◽  
Electronic Transitions ◽  
Photosynthetic Reaction Centers

Observation of ultrafast amorphization dynamics in GeCu2Te3 thin films using echelon-based single-shot transient absorbance spectroscopy

2021 ◽  
Vol 119 (6) ◽  
pp. 061102
Author(s):  
Yusuke Arashida ◽  
Takayuki Suzuki ◽  
Shuhei Nara ◽  
Ikufumi Katayama ◽  
Yasuo Minami ◽  
...  
Keyword(s):  
Thin Films ◽  
Single Shot ◽  
Absorbance Spectroscopy ◽  
Transient Absorbance

scholarly journals Photoinduced Transient Absorbance Spectra of P840/P840+ and the FMO Protein in Reaction Centers of Chlorobium vibrioforme

2001 ◽  
Vol 81 (1) ◽  
pp. 382-393 ◽  
Author(s):  
Ilya R. Vassiliev ◽  
Bodil Kjær ◽  
Gregory L. Schorner ◽  
Henrik V. Scheller ◽  
John H. Golbeck
Keyword(s):  
Reaction Centers ◽  
Chlorobium Vibrioforme ◽  
Fmo Protein ◽  
Transient Absorbance ◽  
Absorbance Spectra

Spectroscopic Study of Interaction of Bare, Citrate Capped and BSA Capped Fe3O4 Nanoparticles with Hemoglobin

2020 ◽  
Vol 13 ◽  
Author(s):  
D. Aich ◽  
S. Saha ◽  
R. N. Mondal ◽  
P. K. Samanta ◽  
T. Kamilya
Keyword(s):  
Amino Acid ◽  
Fe3o4 Nanoparticles ◽  
Fluorescence Emission ◽  
Soret Band ◽  
Acid Group ◽  
Heme Group ◽  
Amino Acid Group ◽  
Absorbance Spectroscopy ◽  
Uv Visible ◽  
Α Helix

Background: Fe3O4nanoparticles have great potential in different biomedical applications. Study of interaction of bare, and capped Fe3O4 nanoparticles with common blood proteins is a field of interest for understanding the underlying mechanism and biocompatibility. Objective: This work is aimed at studying the nature of binding of bare, citrate functionalised and bovine serum albumin coated Fe3O4 nanoparticles (Fe3O4NPs, CFe3O4NPs and BFe3O4NPs) with human hemoglobin (Hb), their instantaneous effect on amino acid group, heme group and secondary structure of Hb. Methods: Nanoparticles were prepared by chemical route and characterised by TEM, XRD and UV-Visible and FTIR spectroscopy. UV-Visible absorbance and fluorescence emission/excitation spectroscopy and circular dichroism were done to study the interaction of nanoparticles with Hb. Results: UV-Visible absorbance spectroscopy shows no blue or red shift of absorption peaks; Benesi-Hildebrand curves for amino acid band and soret band of Hb absorbance spectrum are straight lines with positive intercepts; apparent binding constants and Gibbs free energy change are within moderate level; they are larger for amino acid band in presence of CFe3O4NPs,larger for soret band in presence of Fe3O4NPs,and noticeably small for both bands in presence of BFe3O4NPs.Fluorescence emission/excitation spectra shows no noticeable shift of emission/excitation peak position of Hb in presence of the three nanoparticles. Multiple peak fitting, done for the L-peak of the excitation spectrum of Hb, shows major increase in the percentage of peak area of Tyr in presence of CFe3O4NPs.Circular dichroism measurement shows that CFe3O4NPs, Fe3O4NPs and BFe3O4NPs have reduced the α-helix content of Hb in decreasing order. Conclusion: Ground state complex formation of human hemoglobin with the studied nanoparticles with 1:1 stoichiometric ratio is suggested. Moreover, it is suggested thatCFe3O4NPsmay have stronger interaction with amino acid group while bare Fe3O4NPs may have stronger interaction with the heme group of Hb. Hindering of the energy transfer from tyrosine to tryptophan of Hb in presence of CFe3O4NPs is suggested. CFe3O4NPsmay also have some effect on the secondary structure of Hb as indicated through reduction of the α-helix content. BFe3O4NPshave shown very weak interaction with Hb in UV-Visible absorbance spectroscopy, fluorescence emission/excitation spectroscopy and circular dichroism experiment.

3d-4s and 3d-4p electronic transitions in M2+ : NaF AND M2+ : KMgF3 (Μ = V, Cr, and Mn). Results of a cluster-model calculation

1987 ◽  
Vol 84 ◽  
pp. 855-861 ◽  
Author(s):  
M. Flórez ◽  
M. Bermejo ◽  
V. Luaña ◽  
E. Francisco ◽  
J.M. Recio ◽  
...  
Keyword(s):  
Model Calculation ◽  
Cluster Model ◽  
Electronic Transitions
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