Explorations of the Nonheme High-Valent Iron-Oxo Landscape: Crystal Structure of a Synthetic High-valent Complex with an [FeIV2(mu-O)2] Diamond Core Relevant to the Chemistry of sMMOH

2021 ◽  
Author(s):  
Gregory T Rohde ◽  
Genqiang Xue ◽  
Lawrence Que
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Methanotrophic Bacteria ◽  
High Valent ◽  
Soluble Enzymes

Methanotrophic bacteria utilize methane monooxygenase (MMO) to carry out the first step in metabolizing methane. The soluble enzymes employ a hydroxylase component (sMMOH) with a nonheme diiron active site that...

scholarly journals Crystal Structure, Exogenous Ligand Binding, and Redox Properties of an Engineered Diiron Active Site in a Bacterial Hemerythrin

2013 ◽  
Vol 52 (22) ◽  
pp. 13014-13020 ◽  
Author(s):  
Yasunori Okamoto ◽  
Akira Onoda ◽  
Hiroshi Sugimoto ◽  
Yu Takano ◽  
Shun Hirota ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Active Site ◽  
Redox Properties ◽  
Exogenous Ligand

scholarly journals Crystal Structure of the Dithiol Oxidase DsbA Enzyme fromProteus MirabilisBound Non-covalently to an Active Site Peptide Ligand

2014 ◽  
Vol 289 (28) ◽  
pp. 19810-19822 ◽  
Author(s):  
Fabian Kurth ◽  
Wilko Duprez ◽  
Lakshmanane Premkumar ◽  
Mark A. Schembri ◽  
David P. Fairlie ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Peptide Ligand

WHICH IS THE PROTON-SHUTTLE IN ISOXANTHOPTERIN DEAMINASE? QM/MM MD UNDERSTANDING

2013 ◽  
Vol 12 (08) ◽  
pp. 1341002 ◽  
Author(s):  
XIN ZHANG ◽  
MING LEI
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Proton Transfer ◽  
Glutamic Acid ◽  
Active Site ◽  
Nucleophilic Attack ◽  
Zinc Ions ◽  
Initial Model ◽  
Dynamics Simulations

The deamination process of isoxanthopterin catalyzed by isoxanthopterin deaminase was determined using the combined QM(PM3)/MM molecular dynamics simulations. In this paper, the updated PM3 parameters were employed for zinc ions and the initial model was built up based on the crystal structure. Proton transfer and following steps have been investigated in two paths: Asp336 and His285 serve as the proton shuttle, respectively. Our simulations showed that His285 is more effective than Aap336 in proton transfer for deamination of isoxanthopterin. As hydrogen bonds between the substrate and surrounding residues play a key role in nucleophilic attack, we suggested mutating Thr195 to glutamic acid, which could enhance the hydrogen bonds and help isoxanthopterin get close to the active site. The simulations which change the substrate to pterin 6-carboxylate also performed for comparison. Our results provide reference for understanding of the mechanism of deaminase and for enhancing the deamination rate of isoxanthopterin deaminase.

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