scholarly journals Why Is There an “Inert” Metal Center in the Active Site of Nitrile Hydratase? Reactivity and Ligand Dissociation from a Five-Coordinate Co(III) Nitrile Hydratase Model

2001 ◽  
Vol 123 (3) ◽  
pp. 463-468 ◽  
Author(s):  
Jason Shearer ◽  
Irene Y. Kung ◽  
Scott Lovell ◽  
Werner Kaminsky ◽  
Julie A. Kovacs
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Metal Center ◽  
Ligand Dissociation

scholarly journals Identification of an Active Site-bound Nitrile Hydratase Intermediate through Single Turnover Stopped-flow Spectroscopy

2013 ◽  
Vol 288 (22) ◽  
pp. 15532-15536 ◽  
Author(s):  
Natalie Gumataotao ◽  
Misty L. Kuhn ◽  
Natalia Hajnas ◽  
Richard C. Holz
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Stopped Flow ◽  
Single Turnover

Effect of an Asymmetrically Arranged Equatorial Chelate Ring in an Active Site of Nitrile Hydratase

2008 ◽  
Vol 37 (1) ◽  
pp. 66-67 ◽  
Author(s):  
Takuma Yano ◽  
Yuko Wasada-Tsutsui ◽  
Yuji Kajita ◽  
Tomonori Shibayama ◽  
Yasuhiro Funahasi ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Chelate Ring

Protonation of the Binuclear Metal Center within the Active Site of Phosphotriesterase†

Biochemistry ◽  
2005 ◽  
Vol 44 (33) ◽  
pp. 11005-11013 ◽  
Author(s):  
Cynthia R. Samples ◽  
Timothy Howard ◽  
Frank M. Raushel ◽  
Victoria J. DeRose
Keyword(s):  
Active Site ◽  
Metal Center ◽  
Binuclear Metal

scholarly journals Influence of the Greater Protein Environment on the Electrostatic Potential in Metalloenzyme Active Sites: the Case of Formate Dehydrogenase

2021 ◽  
Author(s):  
Azadeh Nazemi ◽  
Adam Steeves ◽  
Heather Kulik
Keyword(s):  
Electrostatic Potential ◽  
Active Site ◽  
Active Sites ◽  
Formate Dehydrogenase ◽  
Catalyst Design ◽  
Metal Center ◽  
Ambient Conditions ◽  
Shift Analysis ◽  
The Impact ◽  
Protein Environment

The Mo/W containing metalloenzyme formate dehydrogenase (FDH) is an efficient and selective natural catalyst which reversibly converts CO2 to formate under ambient conditions. A greater understanding of the role of the protein environment in determining the local properties of the FDH active site would enable rational bioinspired catalyst design. In this study, we investigate the impact of the greater protein environment on the electrostatic potential (ESP) of the active site. To model the enzyme environment, we used a combination of long-timescale classical molecular dynamics (MD) and multiscale quantum-mechanical/molecular-mechanical (QM/MM) simulations. We leverage the charge shift analysis method to systematically construct QM regions and analyze the electronic environment of the active site by evaluating the degree of charge transfer between the core active site and the protein environment. The contribution of the terminal chalcogen ligand to the ESP of the metal center is substantial and dependent on the chalcogen identity, with ESPs less negative and similar for Se and S terminal chalcogens than for O regardless of whether the Mo6+ or W6+ metal center is present. Our evaluation reveals that the orientation of the sidechains and ligand conformations will alter the relative trends in the ESP observed for a given metal center or terminal chalcogen, highlighting the importance of sampling dynamic fluctuations in the protein. Overall, our observations suggest that the terminal chalcogen ligand identity plays an important role in the enzymatic activity of FDH.

Role of the Amide Carbonyl Groups in the Nitrile Hydratase Active Site for Nitrile Coordination Using Co(III) Complex with N2S3-type Ligand

2015 ◽  
Vol 44 (6) ◽  
pp. 761-763 ◽  
Author(s):  
Takuma Yano ◽  
Tomohiro Ikeda ◽  
Tomonori Shibayama ◽  
Tomohiko Inomata ◽  
Yasuhiro Funahashi ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Carbonyl Groups ◽  
Amide Carbonyl

Iron complexes with an N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase

1997 ◽  
pp. 1711-1712 ◽  
Author(s):  
Alexandre L. Nivorozhkin ◽  
Ali I. Uraev ◽  
Gennadii I. Bondarenko ◽  
Alla S. Antsyshkina ◽  
Vasilii P. Kurbatov ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Iron Complexes ◽  
Hydrolytic Metalloenzyme

scholarly journals Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1

2015 ◽  
Vol 20 (5) ◽  
pp. 885-894 ◽  
Author(s):  
Salette Martinez ◽  
Rui Wu ◽  
Karoline Krzywda ◽  
Veronika Opalka ◽  
Hei Chan ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Comamonas Testosteroni ◽  
Active Site Residues ◽  
Catalytic Role

scholarly journals Non-Tethered Organometallic Phosphonate Inhibitors for Lipase Inhibition: Positioning of the Metal Center in the Active Site of Cutinase

2008 ◽  
Vol 2008 (28) ◽  
pp. 4425-4432 ◽  
Author(s):  
Cornelis A. Kruithof ◽  
Harmen P. Dijkstra ◽  
Martin Lutz ◽  
Anthony L. Spek ◽  
Maarten R. Egmond ◽  
...  
Keyword(s):  
Active Site ◽  
Metal Center ◽  
Lipase Inhibition
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