scholarly journals A two-enzyme cascade reaction consisting of two reaction pathways. Studies in bulk solution for understanding the performance of a flow-through device with immobilised enzymes

RSC Advances ◽  
2020 ◽  
Vol 10 (32) ◽  
pp. 18655-18676 ◽  
Author(s):  
Nicolas Ghéczy ◽  
Kai Sasaki ◽  
Makoto Yoshimoto ◽  
Sajad Pour-Esmaeil ◽  
Martin Kröger ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Horseradish Peroxidase ◽  
Product Formation ◽  
Cascade Reaction ◽  
Reaction Pathways ◽  
Bulk Solution ◽  
Bovine Carbonic Anhydrase ◽  
Enzyme Cascade ◽  
Flow Through ◽  
Immobilised Enzymes

A cascade reaction catalysed by bovine carbonic anhydrase (BCA) and horseradish peroxidase (HRP) proceeds over two possible pathways, which explains differences in product formation for differently immobilised enzymes in flow-through reactions.

Efficient biotransformation and synergetic mechanism of dual-enzyme cascade reaction in nonreducing maltoheptaose synthesis

2021 ◽  
pp. 101066
Author(s):  
Luhua Zheng ◽  
Bo Jiang ◽  
Jingjing Chen ◽  
Tao Zhang ◽  
Xiaohong Gu ◽  
...  
Keyword(s):  
Cascade Reaction ◽  
Enzyme Cascade

Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives

1978 ◽  
Vol 100 (15) ◽  
pp. 4873-4877 ◽  
Author(s):  
I. Bertini ◽  
G. Canti ◽  
C. Luchinat ◽  
A. Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase

Mechanisms of Electrochemical N2 Splitting by a Molybdenum Pincer Complex

2021 ◽  
Author(s):  
Quinton Bruch ◽  
Santanu Malakar ◽  
Alan Goldman ◽  
Alexander Miller
Keyword(s):  
Electrode Surface ◽  
Redox Reactions ◽  
Catalytic Reduction ◽  
Reaction Pathways ◽  
Bulk Solution ◽  
Mechanistic Study ◽  
Pincer Ligands ◽  
Computational Studies ◽  
Pincer Complex ◽  
Bond Scission

Molybdenum complexes supported by tridentate pincer ligands are exceptional catalysts for dinitrogen fixation using chemical reductants, but little is known about their prospects for electrochemical reduction of dinitrogen. The viability of electrochemical N2 binding and splitting by a molybdenum(III) pincer complex, (pyPNP)MoBr3 (pyPNP = 2,6-bis(tBu2PCH2)-C5H3N)), is established in this work, providing a foundation for a detailed mechanistic study of electrode-driven formation of the nitride complex (pyPNP)Mo(N)Br. Electrochemical kinetic analysis, optical and vibrational spectroelectrochemical monitoring, and computational studies point to two reaction pathways: in the “reaction layer” pathway, the molybdenum(III) precursor is reduced by 2e– and generates a bimetallic molybdenum(I) Mo2(-N2) species capable of N–N bond scission. In the “bulk solution” pathway the precursor is reduced by 3e– at the electrode surface to generate molybdenum(0) species that undergo chemical redox reactions via comproportionation in the bulk solution away from the electrode surface to generate the same bimetallic molybdenum(I) species capable of N2 cleavage. The comproportionation reactions reveal the surprising intermediacy of dimolybdenum(0) complex trans,trans-[(pyPNP)Mo(N2)2](-N2) in N2 splitting pathways. The same “over-reduced” molybdenum(0) species was also found to cleave N2 upon addition of lutidinium, an acid frequently used in catalytic reduction of dinitrogen.

scholarly journals Protein Folding by Domain V of Escherichia coli 23S rRNA: Specificity of RNA-Protein Interactions

2008 ◽  
Vol 190 (9) ◽  
pp. 3344-3352 ◽  
Author(s):  
Dibyendu Samanta ◽  
Debashis Mukhopadhyay ◽  
Saheli Chowdhury ◽  
Jaydip Ghosh ◽  
Saumen Pal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Carbonic Anhydrase ◽  
Protein Interactions ◽  
23S Rrna ◽  
Unfolded Proteins ◽  
Bovine Carbonic Anhydrase ◽  
Egg White Lysozyme ◽  
General Protein ◽  
Domain V

ABSTRACT The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.

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