Enzyme Hydration Determines Resistance in Organic Cosolvents

ACS Catalysis ◽  
2020 ◽  
Vol 10 (24) ◽  
pp. 14847-14856
Author(s):  
Haiyang Cui ◽  
Lingling Zhang ◽  
Lobna Eltoukhy ◽  
Qianjia Jiang ◽  
Seval Kübra Korkunç ◽  
...  
Keyword(s):  
Organic Cosolvents

The effect of organic cosolvents on the oxygen affinity of fetal hemoglobin

1991 ◽  
Vol 39 (2) ◽  
pp. 161-169 ◽  
Author(s):  
Valeria Militello ◽  
Eugenio Vitrano ◽  
Antonio Cupane
Keyword(s):  
Oxygen Affinity ◽  
Fetal Hemoglobin ◽  
Organic Cosolvents

scholarly journals Enantioselective Epoxidation by Flavoprotein Monooxygenases Supported by Organic Solvents

Catalysts ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 568 ◽  
Author(s):  
Daniel Eggerichs ◽  
Carolin Mügge ◽  
Julia Mayweg ◽  
Ulf-Peter Apfel ◽  
Dirk Tischler
Keyword(s):  
Organic Solvents ◽  
Nicotinamide Adenine Dinucleotide ◽  
In Silico ◽  
Flavin Adenine Dinucleotide ◽  
Substrate Preference ◽  
Solvent Tolerance ◽  
Organic Cosolvents ◽  
Two Component ◽  
Enantioselective Epoxidation ◽  
Styrene Derivatives

Styrene and indole monooxygenases (SMO and IMO) are two-component flavoprotein monooxygenases composed of a nicotinamide adenine dinucleotide (NADH)-dependent flavin adenine dinucleotide (FAD)-reductase (StyB or IndB) and a monooxygenase (StyA or IndA). The latter uses reduced FAD to activate oxygen and to oxygenate the substrate while releasing water. We circumvented the need for the reductase by direct FAD reduction in solution using the NAD(P)H-mimic 1-benzyl-1,4-dihydronicotinamide (BNAH) to fuel monooxygenases without NADH requirement. Herein, we report on the hitherto unknown solvent tolerance for the indole monooxygenase from Gemmobacter nectariphilus DSM15620 (GnIndA) and the styrene monooxygenase from Gordonia rubripertincta CWB2 (GrStyA). These enzymes were shown to convert bulky and rather hydrophobic styrene derivatives in the presence of organic cosolvents. Subsequently, BNAH-driven biotransformation was furthermore optimized with regard to the applied cosolvent and its concentration as well as FAD and BNAH concentration. We herein demonstrate that GnIndA and GrStyA enable selective epoxidations of allylic double bonds (up to 217 mU mg−1) in the presence of organic solvents such as tetrahydrofuran, acetonitrile, or several alcohols. Notably, GnIndA was found to resist methanol concentrations up to 25 vol.%. Furthermore, a diverse substrate preference was determined for both enzymes, making their distinct use very interesting. In general, our results seem representative for many IMOs as was corroborated by in silico mutagenetic studies.

Effect of organic cosolvents on the free solution mobility of curved and normal DNA molecules

2006 ◽  
Vol 27 (8) ◽  
pp. 1462-1470 ◽  
Author(s):  
Yongjun Lu ◽  
Earle Stellwagen ◽  
Nancy C. Stellwagen
Keyword(s):  
Free Solution ◽  
Dna Molecules ◽  
Organic Cosolvents

Sorption of uranyl(VI) cations on suspended silicate: effects of N-donor ligands, carboxylic acids, organic cosolvents, and metal ions

2007 ◽  
Vol 95 (5) ◽  
Author(s):  
P. N. Pathak ◽  
Gregory R. Choppin
Keyword(s):  
Metal Ions ◽  
Carboxylic Acids ◽  
Uranyl Ion ◽  
Donor Ligands ◽  
Organic Cosolvents

Sorption of uranyl ion, UO

Enzymatic synthesis of chitooligosaccharides in organic cosolvents

2005 ◽  
Vol 37 (6) ◽  
pp. 663-668 ◽  
Author(s):  
Jung Hae Yoon
Keyword(s):  
Enzymatic Synthesis ◽  
Organic Cosolvents

Synthesis of peptide bonds by proteinases. Addition of organic cosolvents shifts peptide bond equilibriums toward synthesis

Biochemistry ◽  
1978 ◽  
Vol 17 (24) ◽  
pp. 5220-5227 ◽  
Author(s):  
Gene A. Homandberg ◽  
Jeffrey A. Mattis ◽  
Michael Laskowski
Keyword(s):  
Peptide Bond ◽  
Peptide Bonds ◽  
Organic Cosolvents

Enhancement of the Conversionof Toluene by Pseudomonas putida F-1 Using Organic Cosolvents

2001 ◽  
Vol 91-93 (1-9) ◽  
pp. 195-204 ◽  
Author(s):  
Miguel Rodriguez, Jr. ◽  
K. Thomas Klasson ◽  
Brian H. Davison
Keyword(s):  
Pseudomonas Putida ◽  
Organic Cosolvents
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