Metal−Substrate Interactions Facilitate the Catalytic Activity of the Bacterial Phosphotriesterase†

Biochemistry ◽  
1996 ◽  
Vol 35 (33) ◽  
pp. 10904-10912 ◽  
Author(s):  
Suk-Bong Hong ◽  
Frank M. Raushel
1982 ◽  
Vol 257 (4) ◽  
pp. 1876-1884 ◽  
Author(s):  
J.D. Lambeth ◽  
S.E. Kitchen ◽  
A.A. Farooqui ◽  
R. Tuckey ◽  
H. Kamin

2020 ◽  
Author(s):  
Rahul Gera ◽  
Kundan K. Singh ◽  
Sayam SenGupta ◽  
Jyotishman Dasgupta

Natural metalloenzymes stabilize reactive intermediates through specific metal-substrate interactions in protein confinement. Using the structural blueprint of enzyme pockets it is possible to trap elusive intermediates inside molecular cavities. Here we demonstrate room temperature trapping of a rare yet stable Fe(IV)-superoxo [FeIV(O2)-bTAML] intermediate subsequent to dioxygen binding at the Fe(III) site of a (Et4N)2[FeIII(Cl)(bTAML)] catalyst confined inside the hydrophobic interior of a water-soluble Pd6L412+ nanocage. <br>


1986 ◽  
Vol 28 (2-3) ◽  
pp. 97-105 ◽  
Author(s):  
Michael D. Bond ◽  
Barton Holmquist ◽  
Bert L. Vallee

2020 ◽  
Author(s):  
Rahul Gera ◽  
Kundan K. Singh ◽  
Sayam SenGupta ◽  
Jyotishman Dasgupta

Natural metalloenzymes stabilize reactive intermediates through specific metal-substrate interactions in protein confinement. Using the structural blueprint of enzyme pockets it is possible to trap elusive intermediates inside molecular cavities. Here we demonstrate room temperature trapping of a rare yet stable Fe(IV)-superoxo [FeIV(O2)-bTAML] intermediate subsequent to dioxygen binding at the Fe(III) site of a (Et4N)2[FeIII(Cl)(bTAML)] catalyst confined inside the hydrophobic interior of a water-soluble Pd6L412+ nanocage. <br>


2021 ◽  
Author(s):  
Magnus Richard Buchner ◽  
Lewis R. Thomas-Hargreaves

Alkaline earth metal catalysis has been a growing field in recent years. To enhance reactivity and to understand the metal-substrate interactions in more detail, reactions are increasingly carried out in...


2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Na Guo ◽  
Yongjie Xi ◽  
Shuanglong Liu ◽  
Chun Zhang

Sign in / Sign up

Export Citation Format

Share Document