scholarly journals Fluorescence Spectroscopy of Porphyrins and Phthalocyanines: Some Insights into Supramolecular Self-Assembly, Microencapsulation, and Imaging Microscopy

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4264
Author(s):  
Raquel Teixeira ◽  
Vanda Vaz Serra ◽  
David Botequim ◽  
Pedro M. R. Paulo ◽  
Suzana M. Andrade ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Steady State ◽  
Bovine Serum Albumin ◽  
Self Assembly ◽  
Spectroscopic Studies ◽  
Pamam Dendrimers ◽  
Dynamic State ◽  
Fluorescence Studies ◽  
J Aggregates ◽  
Molecular Complementarity

The molecular interactions of anionic tetrasulfonate phenyl porphyrin (TPPS) with poly(amido amine) (PAMAM) dendrimers of generation 2.0 and 4.0 (G2 and G4, respectively) forming H- or J-aggregates, as well as with human and bovine serum albumin proteins (HSA and BSA), were reviewed in the context of self-assembly molecular complementarity. The spectroscopic studies were extended to the association of aluminum phthtalocyanine (AlPCS4) detected with a PAMAM G4 dendrimer with fluorescence studies in both steady state and dynamic state, as well as due to the fluorescence quenching associated to electron-transfer with a distribution of lifetimes. The functionalization of TPPS with peripheral substituents enables the assignment of spontaneous pH-induced aggregates with different and well-defined morphologies. Other work reported in the literature, in particular with soft self-assembly materials, fall in the same area with particular interest for the environment. The microencapsulation of TPPS studies into polyelectrolyte capsules was developed quite recently and aroused much interest, which is well supported and complemented by the extensive data reported on the Imaging Microscopy section of the Luminescence of Porphyrins and Phthalocyanines included in the present review.

Spectroscopic Studies on Interaction of Friedelin with Bovine Serum Albumin

2012 ◽  
Vol 18 (2) ◽  
pp. 287
Author(s):  
Zhiwei LIN ◽  
Zhengfu TAI ◽  
Zhongmin WAN ◽  
Fei WANG ◽  
Ningfei LEI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies

Electrochemical behaviour and ESR spectra of nitro substituted mono- and dibenzoylmethylenebenzthiazolines and selenazolines

1979 ◽  
Vol 44 (5) ◽  
pp. 1540-1551 ◽  
Author(s):  
Jaro Komenda ◽  
Jiří Huzlík
Keyword(s):  
Electron Transfer ◽  
Esr Spectroscopy ◽  
Electrochemical Behaviour ◽  
Spectroscopic Studies ◽  
Esr Spectra ◽  
Slow Electron

Compounds of the type of 2-(4'-nitrobenzoyl)methylene-3-ethylbenzothiazoline (I) and 2-bis-(p-nitrobenzoyl)methylene-3-ethylbenzothiazoline (II) were studied polarographically and by ESR spectroscopy to obtain informations about their electrochemical and follow-up reactions and their conformation. Whereas with compounds of the type I the conjugation in their molecules is preserved, with type II the coplanarity of the molecules is disturbed, which is manifested in the values of the splitting constants of the ESR spectra and a slow electron transfer between both nitrophenyl substituents. These conclusions are supported by NMR spectroscopic studies.

In situ fabrication of PHEMA–BSA core–corona biohybrid particles

2016 ◽  
Vol 4 (25) ◽  
pp. 4430-4438 ◽  
Author(s):  
Jin-Tao Wang ◽  
Yanhang Hong ◽  
Xiaotian Ji ◽  
Mingming Zhang ◽  
Li Liu ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Atom Transfer ◽  
Hydroxyethyl Methacrylate ◽  
In Situ Fabrication ◽  
Radical Polymerizations

Poly(2-hydroxyethyl methacrylate)–bovine serum albumin core–corona particles were prepared using in situ activators generated by electron transfer for atom transfer radical polymerizations of HEMA initiated by a BSA macroinitiator.

scholarly journals The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2

1993 ◽  
Vol 291 (1) ◽  
pp. 89-94 ◽  
Author(s):  
P White ◽  
F D C Manson ◽  
C E Brunt ◽  
S K Chapman ◽  
G A Reid
Keyword(s):  
Electron Transfer ◽  
Steady State ◽  
Cytochrome C ◽  
Kinetic Properties ◽  
Stopped Flow ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Cytochrome C Reductase ◽  
Flavocytochrome B2 ◽  
Cytochrome C Reduction

The two distinct domains of flavocytochrome b2 (L-lactate:cytochrome c oxidoreductase) are connected by a typical hinge peptide. The amino acid sequence of this interdomain hinge is dramatically different in flavocytochromes b2 from Saccharomyces cerevisiae and Hansenula anomala. This difference in the hinge is believed to contribute to the difference in kinetic properties between the two enzymes. To probe the importance of the hinge, an interspecies hybrid enzyme has been constructed comprising the bulk of the S. cerevisiae enzyme but containing the H. anomala flavocytochrome b2 hinge. The kinetic properties of this ‘hinge-swap’ enzyme have been investigated by steady-state and stopped-flow methods. The hinge-swap enzyme remains a good lactate dehydrogenase as is evident from steady-state experiments with ferricyanide as acceptor (only 3-fold less active than wild-type enzyme) and stopped-flow experiments monitoring flavin reduction (2.5-fold slower than in wild-type enzyme). The major effect of the hinge-swap mutation is to lower dramatically the enzyme's effectiveness as a cytochrome c reductase; kcat. for cytochrome c reduction falls by more than 100-fold, from 207 +/- 10 s-1 (25 degrees C, pH 7.5) in the wild-type enzyme to 1.62 +/- 0.41 s-1 in the mutant enzyme. This fall in cytochrome c reductase activity results from poor interdomain electron transfer between the FMN and haem groups. This can be demonstrated by the fact that the kcat. for haem reduction in the hinge-swap enzyme (measured by the stopped-flow method) has a value of 1.61 +/- 0.42 s-1, identical with the value for cytochrome c reduction and some 300-fold lower than the value for the wild-type enzyme. From these and other kinetic parameters, including kinetic isotope effects with [2-2H]lactate, we conclude that the hinge plays a crucial role in allowing efficient electron transfer between the two domains of flavocytochrome b2.

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