Comparison of separation behavior of Ir(IV) and Rh(III) between tin(II) chloride and ascorbic acid as a reducing agent in the extraction with Cyanex 921 and Cyanex 301

2018 ◽  
Vol 36 (3) ◽  
pp. 272-285 ◽  
Author(s):  
Minh Nhan Le ◽  
Thi Hong Nguyen ◽  
Man Seung Lee
Keyword(s):  
Ascorbic Acid ◽  
Reducing Agent ◽  
Cyanex 301 ◽  
Cyanex 921 ◽  
Separation Behavior

Ascorbic acid as a reducing agent in quantitative analysis

1956 ◽  
Vol 150 (1) ◽  
pp. 29-39 ◽  
Author(s):  
G. Gopala Rao ◽  
U. Veereswara Rao
Keyword(s):  
Ascorbic Acid ◽  
Quantitative Analysis ◽  
Reducing Agent

Aqueous synthesis of luminescent cadmium telluride quantum dots using ascorbic acid as the reducing agent

2014 ◽  
Vol 9 (7) ◽  
pp. 478-481 ◽  
Author(s):  
Xian Xie ◽  
Xiaoyu Wu ◽  
Tangkang Liu ◽  
Huaimei Li ◽  
Yilin Wang ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Ascorbic Acid ◽  
Cadmium Telluride ◽  
Reducing Agent ◽  
Aqueous Synthesis ◽  
Cadmium Telluride Quantum Dots

Green synthesis of a silver nanoparticle–graphene oxide composite and its application for As(iii) detection

RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14432-14440 ◽  
Author(s):  
Riyaz Ahmad Dar ◽  
Ninad G. Khare ◽  
Daniel P. Cole ◽  
Shashi P. Karna ◽  
Ashwini Kumar Srivastava
Keyword(s):  
Ascorbic Acid ◽  
Graphene Oxide ◽  
Green Synthesis ◽  
Silver Nanoparticle ◽  
Reducing Agent ◽  
Synthetic Approach ◽  
Stabilizing Agent ◽  
Oxide Composite ◽  
Beta Cyclodextrin

We report a facile and green synthetic approach to synthesize a silver nanoparticle (AgNPs)–graphene oxide (GO) composite using beta cyclodextrin as a stabilizing agent and ascorbic acid as a reducing agent.

scholarly journals The mechanism of reduction of single-site redox proteins by ascorbic acid

1979 ◽  
Vol 177 (2) ◽  
pp. 641-648 ◽  
Author(s):  
A I Al-Ayash ◽  
M T Wilson
Keyword(s):  
Ascorbic Acid ◽  
Rate Constants ◽  
Activation Parameters ◽  
Outer Sphere ◽  
Reducing Agent ◽  
Second Order ◽  
Single Site ◽  
Redox Proteins ◽  
Order Rate ◽  
Temperature Dependences

The reduction of single-site haem and copper redox proteins by ascorbic acid was studied as a function of pH. Evidence is presented that indicates that the double-deprotonated ascorbate anion, ascorbate2-, is the reducing agent, and the pH-independent second-order rate constants for reduction by this species are given. Investigation of the temperature dependences of these rate constants have yielded the values of the activation parameters (delta H++ and delta S++) for reduction. These values, together with ligand-replacement studies, suggest that ascorbate2- acts as an outer-sphere reductant for these proteins. Reasons to account for the apparent inability of ascorbic acid to reduce the alkaline conformer of mammalian ferricytochrome c are suggested.

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