scholarly journals Chiral recognition of prochiral centres and general acid-base catalysis. Necessarily interrelated manifestations of active-site structure

1976 ◽  
Vol 153 (2) ◽  
pp. 491-493 ◽  
Author(s):  
J Südi
Keyword(s):  
Lactate Dehydrogenase ◽  
Active Site ◽  
Chiral Recognition ◽  
Conformational Transition ◽  
Base Catalysis ◽  
Acid Base ◽  
Site Structure ◽  
General Acid ◽  
Active Site Structure

On the basis of Ogston's [(1948) Nature (London) 162, 963] argument, the following conclusions are indicated by the stereochemistry of the reversible oxidation of glycollate by lactate dehydrogenase: (1) general acid-base catalysis is involved in the reaction; (2) the transformation of enzyme-bound (tetrahedral) substrate into enzyme-bound (trigonal) product involves a conformational transition of the enzyme-coenzyme complex.

General Acid/Base Catalysis in the Active Site ofEscherichia coliThioredoxin†

Biochemistry ◽  
1997 ◽  
Vol 36 (50) ◽  
pp. 15810-15816 ◽  
Author(s):  
Peter T. Chivers ◽  
Ronald T. Raines
Keyword(s):  
Active Site ◽  
Base Catalysis ◽  
Acid Base ◽  
General Acid

Active site structure and catalytic mechanisms of human peroxidases

2006 ◽  
Vol 445 (2) ◽  
pp. 199-213 ◽  
Author(s):  
Paul G. Furtmüller ◽  
Martina Zederbauer ◽  
Walter Jantschko ◽  
Jutta Helm ◽  
Martin Bogner ◽  
...  
Keyword(s):  
Active Site ◽  
Site Structure ◽  
Active Site Structure ◽  
Catalytic Mechanisms

scholarly journals Iron-Imprinted Single-Atomic Site Catalyst-Based Nanoprobe for Detection of Hydrogen Peroxide in Living Cells

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Zhaoyuan Lyu ◽  
Shichao Ding ◽  
Maoyu Wang ◽  
Xiaoqing Pan ◽  
Zhenxing Feng ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Single Atom ◽  
Site Structure ◽  
Atomic Site ◽  
Ion Imprinting ◽  
Active Site Structure ◽  
In Situ Detection ◽  
Colorimetric Biosensing

AbstractFe-based single-atomic site catalysts (SASCs), with the natural metalloproteases-like active site structure, have attracted widespread attention in biocatalysis and biosensing. Precisely, controlling the isolated single-atom Fe-N-C active site structure is crucial to improve the SASCs’ performance. In this work, we use a facile ion-imprinting method (IIM) to synthesize isolated Fe-N-C single-atomic site catalysts (IIM-Fe-SASC). With this method, the ion-imprinting process can precisely control ion at the atomic level and form numerous well-defined single-atomic Fe-N-C sites. The IIM-Fe-SASC shows better peroxidase-like activities than that of non-imprinted references. Due to its excellent properties, IIM-Fe-SASC is an ideal nanoprobe used in the colorimetric biosensing of hydrogen peroxide (H2O2). Using IIM-Fe-SASC as the nanoprobe, in situ detection of H2O2 generated from MDA-MB-231 cells has been successfully demonstrated with satisfactory sensitivity and specificity. This work opens a novel and easy route in designing advanced SASC and provides a sensitive tool for intracellular H2O2 detection.

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