Switching Redox-Active Sites by Valence Tautomerism in Prussian Blue Analogues AxMny[Fe(CN)6]·nH2O (A: K, Rb): Robust Frameworks for Reversible Li Storage

2010 ◽  
Vol 1 (14) ◽  
pp. 2063-2071 ◽  
Author(s):  
M. Okubo ◽  
D. Asakura ◽  
Y. Mizuno ◽  
J.-D. Kim ◽  
T. Mizokawa ◽  
...  
Keyword(s):  
Prussian Blue ◽  
Active Sites ◽  
Valence Tautomerism ◽  
Prussian Blue Analogues ◽  
Redox Active ◽  
Li Storage

Design and Synthesis of Concentration Gradient Prussian Blue Analogues

2021 ◽  
Vol 21 (2) ◽  
pp. 916-925
Author(s):  
SuKyung Jeon ◽  
Carissa H. Li ◽  
Daniel R. Talham
Keyword(s):  
Prussian Blue ◽  
Concentration Gradient ◽  
Design And Synthesis ◽  
Prussian Blue Analogues

Titelbild: Mesostructured Prussian Blue Analogues (Angew. Chem. 3/2008)

2007 ◽  
Vol 120 (3) ◽  
pp. 427-427
Author(s):  
Xavier Roy ◽  
Laurence K. Thompson ◽  
Neil Coombs ◽  
Mark J. MacLachlan
Keyword(s):  
Prussian Blue ◽  
Prussian Blue Analogues

scholarly journals Conjugate of Thiol and Guanidyl Units with Oligoethylene Glycol Linkage for Manipulation of Oxidative Protein Folding

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 879
Author(s):  
Shunsuke Okada ◽  
Motonori Matsusaki ◽  
Masaki Okumura ◽  
Takahiro Muraoka
Keyword(s):  
Protein Folding ◽  
Active Sites ◽  
Biological Process ◽  
Thiol Group ◽  
Native Conformation ◽  
Thiol Compounds ◽  
Oxidative Protein Folding ◽  
Redox Active ◽  
A Cell ◽  
Protein Disulfide

Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues. In a cell, disulfide-catalysts such as protein disulfide isomerase promote the oxidative protein folding. Inspired by the active sites of the disulfide-catalysts, synthetic redox-active thiol compounds have been developed, which have shown significant promotion of the folding processes. In our previous study, coupling effects of a thiol group and guanidyl unit on the folding promotion were reported. Herein, we investigated the influences of a spacer between the thiol group and guanidyl unit. A conjugate between thiol and guanidyl units with a diethylene glycol spacer (GdnDEG-SH) showed lower folding promotion effect compared to the thiol–guanidyl conjugate without the spacer (GdnSH). Lower acidity and a more reductive property of the thiol group of GdnDEG-SH compared to those of GdnSH likely resulted in the reduced efficiency of the folding promotion. Thus, the spacer between the thiol and guanidyl groups is critical for the promotion of oxidative protein folding.

scholarly journals “Green” Prussian Blue Analogues as Peroxidase Mimetics for Amperometric Sensing and Biosensing

Biosensors ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 193
Author(s):  
Galina Z. Gayda ◽  
Olha M. Demkiv ◽  
Yanna Gurianov ◽  
Roman Ya. Serkiz ◽  
Halyna M. Klepach ◽  
...  
Keyword(s):  
Prussian Blue ◽  
Noble Metals ◽  
High Sensitivity ◽  
Graphite Electrodes ◽  
Flavocytochrome B2 ◽  
Prussian Blue Analogues ◽  
Scientific Investigations ◽  
Electrochemically Active ◽  
Amperometric Sensing ◽  
Prussian Blue Analogs

Prussian blue analogs (PBAs) are well-known artificial enzymes with peroxidase (PO)-like activity. PBAs have a high potential for applications in scientific investigations, industry, ecology and medicine. Being stable and both catalytically and electrochemically active, PBAs are promising in the construction of biosensors and biofuel cells. The “green” synthesis of PO-like PBAs using oxido-reductase flavocytochrome b2 is described in this study. When immobilized on graphite electrodes (GEs), the obtained green-synthesized PBAs or hexacyanoferrates (gHCFs) of transition and noble metals produced amperometric signals in response to H2O2. HCFs of copper, iron, palladium and other metals were synthesized and characterized by structure, size, catalytic properties and electro-mediator activities. The gCuHCF, as the most effective PO mimetic with a flower-like micro/nano superstructure, was used as an H2O2-sensitive platform for the development of a glucose oxidase (GO)-based biosensor. The GO/gCuHCF/GE biosensor exhibited high sensitivity (710 A M−1m−2), a broad linear range and good selectivity when tested on real samples of fruit juices. We propose that the gCuHCF and other gHCFs synthesized via enzymes may be used as artificial POs in amperometric oxidase-based (bio)sensors.

Bonding properties in Prussian blue analogues of the type Fe[Fe(CN)5X]·xH2O

1979 ◽  
Vol 41 (3) ◽  
pp. 287-292 ◽  
Author(s):  
E. Fluck ◽  
H. Inoue ◽  
M. Nagao ◽  
S. Yanagisawa
Keyword(s):  
Prussian Blue ◽  
Prussian Blue Analogues ◽  
Bonding Properties
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