scholarly journals Role of the Support and Reaction Conditions on the Vapor-Phase Deoxygenation of m-Cresol over Pt/C and Pt/TiO2 Catalysts

ACS Catalysis ◽  
2016 ◽  
Vol 6 (4) ◽  
pp. 2715-2727 ◽  
Author(s):  
Michael B. Griffin ◽  
Glen A. Ferguson ◽  
Daniel A. Ruddy ◽  
Mary J. Biddy ◽  
Gregg T. Beckham ◽  
...  
Keyword(s):  
Vapor Phase ◽  
Reaction Conditions

scholarly journals Supercritical Carbon Dioxide Effect on Lipase-Catalyzed Geranyl Acetate Synthesis

2022 ◽  
Author(s):  
Matheus Tavares ◽  
Luís Kanda ◽  
Wanderson Giacomin Júnior ◽  
Luiz Ramos ◽  
Luciana Vandenberghe ◽  
...  
Keyword(s):  
Carbon Dioxide ◽  
Supercritical Fluids ◽  
Vapor Phase ◽  
Supercritical Co2 ◽  
Geranyl Acetate ◽  
Similar Reaction ◽  
Reaction Conditions ◽  
Phase Extension ◽  
One Step

This work provides a general insight on lipase-catalyzed synthesis of geranyl acetate through esterification of geraniol with acetic acid. Although this reaction is relatively well known, the replacement of organic solvents by supercritical fluids is fairly recent and the role of CO2 is still not completely understood. Therefore, reactions were performed with Lipozyme® RM IM and Novozym® 435 as biocatalysts, and hexane and CO2 as solvents. For similar reaction conditions, geraniol conversions obtained using hexane were much higher, rather than supercritical CO2 (scCO2, 82.9% versus 12.0% after 4 h). The results obtained indicated that CO2 might help the migration of water from the enzyme surface to reaction bulk and then to the vapor phase. Thus, by increasing the vapor phase extension, the geraniol conversion enhanced to 60.5% after 4 h. Such improvement represents one step forward to comprehend the influence of CO2, a safer and greener solvent as compared to hexane.

Microbial Bioconversion: A Regio-specific Method for Novel Drug Design and Toxicological Study of Metabolites

2019 ◽  
Vol 20 (14) ◽  
pp. 1156-1162
Author(s):  
Maria Yousuf ◽  
Waqas Jamil ◽  
Khayala Mammadova
Keyword(s):  
Microbial Transformation ◽  
Specific Method ◽  
Reaction Conditions ◽  
Small Organic Molecules ◽  
Toxicological Studies ◽  
Drug Designing ◽  
Transformation Methods ◽  
Novel Drug

The methods of chemical structural alteration of small organic molecules by using microbes (fungi, bacteria, yeast, etc.) are gaining tremendous attention to obtain structurally novel and therapeutically potential leads. The regiospecific mild environmental friendly reaction conditions with the ability of novel chemical structural modification in compounds categorize this technique; a distinguished and unique way to obtain medicinally important drugs and their in vivo mimic metabolites with costeffective and timely manner. This review article shortly addresses the immense pharmaceutical importance of microbial transformation methods in drug designing and development as well as the role of CYP450 enzymes in fungi to obtain in vivo drug metabolites for toxicological studies.

TBAI Catalyzed Electrochemical C-H Bond Activation of 2-arylated-N-methoxyamides for the Synthesis of Phenanthridinones

Synlett ◽  
2021 ◽  
Author(s):  
Kripa Subramanian ◽  
Subhash L. Yedage ◽  
Kashish Sethi ◽  
Bhalchandra M. Bhanage
Keyword(s):  
Electrochemical Method ◽  
Bond Activation ◽  
Supporting Electrolyte ◽  
Bioactive Compound ◽  
Reaction Conditions ◽  
Redox Catalyst ◽  
Synthetic Utility ◽  
One Step ◽  
Constant Potential

An electrochemical method for the synthesis of phenanthridinones via constant potential electrolysis (CPE) mediated by <i>n</i>-Bu<sub>4</sub>NI (TBAI) has been reported. The protocol is metal and oxidant free and proceeds with 100% current efficiency. Here TBAI plays the dual role of the redox catalyst as well as supporting electrolyte. The intramolecular C-H activation proceeds under mild reaction conditions and short reaction time via electrochemically generated amidyl radicals. The reaction has been scaled up to gram level showing its practicability and the synthetic utility and applicability of the protocol has been demonstrated by the direct one-step synthesis of the bioactive compound Phenaglaydon.

N-Chlorinative Ring Contraction of 1,4-Dimethoxyphthalazines via a Bicyclization/Ring-Opening Mechanism

Synthesis ◽  
2020 ◽  
Author(s):  
Jeong Kyun Im ◽  
Ilju Jeong ◽  
Jun-Ho Choi ◽  
Won-jin Chung ◽  
ByeongDo Yang ◽  
...  
Keyword(s):  
Ring Opening ◽  
Reaction Conditions ◽  
Ring Contraction ◽  
Silyl Group ◽  
Favorskii Rearrangement ◽  
Mechanistic Analysis ◽  
Group A ◽  
Overall Efficiency ◽  
Trichloroisocyanuric Acid

AbstractAn unprecedented N-chlorinative ring contraction of 1,2-diazines was discovered and investigated with an electrophilic chlorinating reagent, trichloroisocyanuric acid (TCICA). Through optimization and mechanistic analysis, the assisting role of n-Bu4NCl as an exogenous nucleophile was identified, and the optimized reaction conditions were applied to a range of 1,4-dimethoxyphthalazine derivatives. Also, an improvement of overall efficiency was demonstrated by the use of a labile O-silyl group. A bicyclization/ring-opening mechanism, inspired by the Favorskii rearrangement, was proposed and supported by the DFT calculations. Furthermore, the efforts on scope expansion as well as the evaluation of other electrophilic promoters revealed that the newly developed ring contraction reactivity is a unique characteristic of 1,4-dimethoxyphthalazine scaffold and TCICA.

scholarly journals Enzymatic synthesis and phosphorolysis of 4(2)-thioxo- and 6(5)-azapyrimidine nucleosides by E. coli nucleoside phosphorylases

2016 ◽  
Vol 12 ◽  
pp. 2588-2601 ◽  
Author(s):  
Vladimir A Stepchenko ◽  
Anatoly I Miroshnikov ◽  
Frank Seela ◽  
Igor A Mikhailopulo
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Reaction Conditions ◽  
E Coli ◽  
No Formation ◽  
Structural Peculiarities ◽  
Substrate Properties ◽  
Nucleoside Phosphorylases ◽  
Derivatives Of

The trans-2-deoxyribosylation of 4-thiouracil (4SUra) and 2-thiouracil (2SUra), as well as 6-azauracil, 6-azathymine and 6-aza-2-thiothymine was studied using dG and E. coli purine nucleoside phosphorylase (PNP) for the in situ generation of 2-deoxy-α-D-ribofuranose-1-phosphate (dRib-1P) followed by its coupling with the bases catalyzed by either E. coli thymidine (TP) or uridine (UP) phosphorylases. 4SUra revealed satisfactory substrate activity for UP and, unexpectedly, complete inertness for TP; no formation of 2’-deoxy-2-thiouridine (2SUd) was observed under analogous reaction conditions in the presence of UP and TP. On the contrary, 2SU, 2SUd, 4STd and 2STd are good substrates for both UP and TP; moreover, 2SU, 4STd and 2’-deoxy-5-azacytidine (Decitabine) are substrates for PNP and the phosphorolysis of the latter is reversible. Condensation of 2SUra and 5-azacytosine with dRib-1P (Ba salt) catalyzed by the accordant UP and PNP in Tris∙HCl buffer gave 2SUd and 2’-deoxy-5-azacytidine in 27% and 15% yields, respectively. 6-Azauracil and 6-azathymine showed good substrate properties for both TP and UP, whereas only TP recognizes 2-thio-6-azathymine as a substrate. 5-Phenyl and 5-tert-butyl derivatives of 6-azauracil and its 2-thioxo derivative were tested as substrates for UP and TP, and only 5-phenyl- and 5-tert-butyl-6-azauracils displayed very low substrate activity. The role of structural peculiarities and electronic properties in the substrate recognition by E. coli nucleoside phosphorylases is discussed.

Role of Vapor Phase in Oxidation/Combustion Kinetics of High-Pressure Air Injection (HPAI)

2010 ◽  
Author(s):  
Yalda Barzin ◽  
Robert Gordon Moore ◽  
Sudarshan A. Mehta ◽  
Don G. Mallory ◽  
Matthew G. Ursenbach ◽  
...  
Keyword(s):  
High Pressure ◽  
Vapor Phase ◽  
Air Injection ◽  
Combustion Kinetics ◽  
Kinetics Of

Peroxovanadates and Its Bio-Mimicking Relation with Vanadium Haloperoxidases

2016 ◽  
pp. 197-219
Author(s):  
Pranjal Saikia ◽  
Saitanya Kumar Bharadwaj ◽  
Abu Taleb Miah
Keyword(s):  
Amino Acids ◽  
Active Site ◽  
High Efficiency ◽  
Recombinant Enzymes ◽  
Vanadium Compounds ◽  
Reaction Conditions ◽  
The Cost ◽  
Major Emphasis ◽  
Protein Active Site

Vanadium Haloperoxidases (VHPOs) have been used in a variety of biotransformations showing remarkable stereoselectivity and regiospecificity. The high efficiency of the enzyme is influenced by the protein active site and the role of certain amino acids in activation of vanadium(V)-bound peroxide for halide oxidation. The use of natural or recombinant enzymes, or biomimetic vanadium compounds brings up issues regarding the cost of production and reaction conditions. In this chapter, the primary intent is to provide a simple and clear picture of functional mimicking nature of peroxovanadium compounds with haloperoxidases enzymes to the readers. Major emphasis would be given to examine the reactivity of the vanadium haloperoxidases with mechanism.

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