scholarly journals Interaction of Potassium Cyanide with the [Ni-4Fe-5S] Active Site Cluster of CO Dehydrogenase fromCarboxydothermus hydrogenoformans

2007 ◽  
Vol 282 (14) ◽  
pp. 10639-10646 ◽  
Author(s):  
Seung-Wook Ha ◽  
Malgorzata Korbas ◽  
Mirjam Klepsch ◽  
Wolfram Meyer-Klaucke ◽  
Ortwin Meyer ◽  
...  
Keyword(s):  
Active Site ◽  
Potassium Cyanide ◽  
Co Dehydrogenase ◽  
Site Cluster

Nickel(II) in an almost regular tetrahedral thiolate environment: a first generation synthetic analogue of the active site of nickel CO-dehydrogenase

2001 ◽  
pp. 1387-1388 ◽  
Author(s):  
Matt C. Smith ◽  
Steven Longhurst ◽  
J. Elaine Barclay ◽  
Stephen P. Cramer ◽  
Sian C. Davies ◽  
...  
Keyword(s):  
Active Site ◽  
First Generation ◽  
Synthetic Analogue ◽  
Co Dehydrogenase

scholarly journals Converting the NiFeS Carbon Monoxide Dehydrogenase to a Hydrogenase and a Hydroxylamine Reductase

2002 ◽  
Vol 184 (21) ◽  
pp. 5894-5897 ◽  
Author(s):  
Jongyun Heo ◽  
Marcus T. Wolfe ◽  
Christopher R. Staples ◽  
Paul W. Ludden
Keyword(s):  
Carbon Monoxide ◽  
Amino Acid ◽  
Active Site ◽  
Reductase Activity ◽  
Carbon Monoxide Dehydrogenase ◽  
Hydrogenase Activity ◽  
Uptake Hydrogenase ◽  
Site Cluster ◽  
Metal Ligand

ABSTRACT Substitution of one amino acid for another at the active site of an enzyme usually diminishes or eliminates the activity of the enzyme. In some cases, however, the specificity of the enzyme is changed. In this study, we report that the changing of a metal ligand at the active site of the NiFeS-containing carbon monoxide dehydrogenase (CODH) converts the enzyme to a hydrogenase or a hydroxylamine reductase. CODH with alanine substituted for Cys531 exhibits substantial uptake hydrogenase activity, and this activity is enhanced by treatment with CO. CODH with valine substituted for His265 exhibits hydroxylamine reductase activity. Both Cys531 and His265 are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity.

scholarly journals Understanding the role of active site residues in CotB2 catalysis using a cluster model

2020 ◽  
Vol 16 ◽  
pp. 50-59 ◽  
Author(s):  
Keren Raz ◽  
Ronja Driller ◽  
Thomas Brück ◽  
Bernhard Loll ◽  
Dan T Major
Keyword(s):  
Gas Phase ◽  
Active Site ◽  
Cluster Model ◽  
Electronic Energy ◽  
Active Site Residues ◽  
Multistep Synthesis ◽  
Site Cluster ◽  
Phase Data ◽  
Streptomyces Melanosporofaciens

Terpene cyclases are responsible for the initial cyclization cascade in the multistep synthesis of a large number of terpenes. CotB2 is a diterpene cyclase from Streptomyces melanosporofaciens, which catalyzes the formation of cycloocta-9-en-7-ol, a precursor to the next-generation anti-inflammatory drug cyclooctatin. In this work, we present evidence for the significant role of the active site's residues in CotB2 on the reaction energetics using quantum mechanical calculations in an active site cluster model. The results revealed the significant effect of the active site residues on the relative electronic energy of the intermediates and transition state structures with respect to gas phase data. A detailed understanding of the role of the enzyme environment on the CotB2 reaction cascade can provide important information towards a biosynthetic strategy for cyclooctatin and the biomanufacturing of related terpene structures.

Carbon Monoxide Induced Decomposition of the Active Site [Ni−4Fe−5S] Cluster of CO Dehydrogenase

2004 ◽  
Vol 126 (17) ◽  
pp. 5382-5387 ◽  
Author(s):  
Holger Dobbek ◽  
Vitali Svetlitchnyi ◽  
Jago Liss ◽  
Ortwin Meyer
Keyword(s):  
Carbon Monoxide ◽  
Active Site ◽  
Co Dehydrogenase ◽  
Induced Decomposition

scholarly journals QM/MM study of the binding of H2 to MoCu CO dehydrogenase: development and applications of improved H2 van der Waals parameters

2021 ◽  
Vol 27 (3) ◽  
Author(s):  
Anna Rovaletti ◽  
Claudio Greco ◽  
Ulf Ryde
Keyword(s):  
Active Site ◽  
Hydrogen Oxidation ◽  
Van Der Waals ◽  
Oxidation Mechanism ◽  
Oxidation Catalysis ◽  
Hydrogenase Activity ◽  
Binding Modes ◽  
Co Dehydrogenase ◽  
Enzyme Active Site ◽  
New Perspective

AbstractThe MoCu CO dehydrogenase enzyme not only transforms CO into CO2 but it can also oxidise H2. Even if its hydrogenase activity has been known for decades, a debate is ongoing on the most plausible mode for the binding of H2 to the enzyme active site and the hydrogen oxidation mechanism. In the present work, we provide a new perspective on the MoCu-CODH hydrogenase activity by improving the in silico description of the enzyme. Energy refinement—by means of the BigQM approach—was performed on the intermediates involved in the dihydrogen oxidation catalysis reported in our previously published work (Rovaletti, et al. “Theoretical Insights into the Aerobic Hydrogenase Activity of Molybdenum–Copper CO Dehydrogenase.” Inorganics 7 (2019) 135). A suboptimal description of the H2–HN(backbone) interaction was observed when the van der Waals parameters described in previous literature for H2 were employed. Therefore, a new set of van der Waals parameters is developed here in order to better describe the hydrogen–backbone interaction. They give rise to improved binding modes of H2 in the active site of MoCu CO dehydrogenase. Implications of the resulting outcomes for a better understanding of hydrogen oxidation catalysis mechanisms are proposed and discussed.

scholarly journals Understanding the Role of Active Site Residues in CotB2 Catalysis Using a Cluster Model

2019 ◽  
Author(s):  
Keren Raz ◽  
Ronja Driller ◽  
Thomas Brück ◽  
Bernhard Loll ◽  
Dan Thomas Major
Keyword(s):  
Active Site ◽  
Cluster Model ◽  
Electronic Energy ◽  
Active Site Residues ◽  
Site Model ◽  
Multistep Synthesis ◽  
Active Site Model ◽  
Site Cluster ◽  
Phase Data

Terpene cyclases are responsible for the initial cyclization cascade in the multistep synthesis of a large number of terpenes. CotB2 is a diterpene cyclase from Streptomyces melanosporofaciens, which synthesizes the formation of cyclooctat-9-en-7-ol, a precursor to the next-generation anti-inflammatory drug, cyclooctatin. In this work, we present evidence for a significant role of the active site residues in CotB2 on the reaction energetics using quantum mechanics calculations in an active site cluster model. The results using the active site model reveal the significant effect of the active site residues on the relative electronic energy of the intermediates and transition state (TS) structures with respect to gas phase data. A detailed understanding of the role of the enzyme environment on the CotB2 reaction cascade can provide important information towards a biosynthetic strategy for cyclooctatin and the biomanufacturing of related terpene structures.

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