Olefin metathesis over well-defined active fixed molybdenum catalysts. Structure and oxidation state of the active site and reaction mechanism

1981 ◽  
Vol 77 (8) ◽  
pp. 1763 ◽  
Author(s):  
Yasuhiro Iwasawa ◽  
Hiroshi Ichinose ◽  
Sadao Ogasawara ◽  
Mitsuyuki Soma
Keyword(s):  
Reaction Mechanism ◽  
Oxidation State ◽  
Active Site ◽  
Olefin Metathesis ◽  
Molybdenum Catalysts

The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities

2014 ◽  
Vol 70 (12) ◽  
pp. 3212-3225 ◽  
Author(s):  
Tiila-Riikka Kiema ◽  
Rajesh K. Harijan ◽  
Malgorzata Strozyk ◽  
Toshiyuki Fukao ◽  
Stefan E. H. Alexson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism ◽  
Active Site ◽  
Quaternary Structure ◽  
Fatty Acyl ◽  
Physiological Importance ◽  
Loop Domain ◽  
Solution Studies ◽  
Hydrolysis Of ◽  
Insight Into

Crystal structures of human mitochondrial 3-ketoacyl-CoA thiolase (hT1) in the apo form and in complex with CoA have been determined at 2.0 Å resolution. The structures confirm the tetrameric quaternary structure of this degradative thiolase. The active site is surprisingly similar to the active site of theZoogloea ramigerabiosynthetic tetrameric thiolase (PDB entries 1dm3 and 1m1o) and different from the active site of the peroxisomal dimeric degradative thiolase (PDB entries 1afw and 2iik). A cavity analysis suggests a mode of binding for the fatty-acyl tail in a tunnel lined by the Nβ2–Nα2 loop of the adjacent subunit and the Lα1 helix of the loop domain. Soaking of the apo hT1 crystals with octanoyl-CoA resulted in a crystal structure in complex with CoA owing to the intrinsic acyl-CoA thioesterase activity of hT1. Solution studies confirm that hT1 has low acyl-CoA thioesterase activity for fatty acyl-CoA substrates. The fastest rate is observed for the hydrolysis of butyryl-CoA. It is also shown that T1 has significant biosynthetic thiolase activity, which is predicted to be of physiological importance.

scholarly journals Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase

2017 ◽  
Vol 139 (29) ◽  
pp. 9927-9936 ◽  
Author(s):  
William E. Robinson ◽  
Arnau Bassegoda ◽  
Erwin Reisner ◽  
Judy Hirst
Keyword(s):  
Oxidation State ◽  
Active Site ◽  
Formate Dehydrogenase ◽  
Binding Properties ◽  
State Dependent

scholarly journals Reaction Mechanism of the ε Subunit ofE. coliDNA Polymerase III: Insights into Active Site Metal Coordination and Catalytically Significant Residues

2009 ◽  
Vol 131 (4) ◽  
pp. 1550-1556 ◽  
Author(s):  
G. Andrés Cisneros ◽  
Lalith Perera ◽  
Roel M. Schaaper ◽  
Lars C. Pedersen ◽  
Robert E. London ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Active Site ◽  
Metal Coordination ◽  
Polymerase Iii

scholarly journals Structural evidence for the covalent modification of FabH by 4,5-dichloro-1,2-dithiol-3-one (HR45)

2017 ◽  
Vol 15 (30) ◽  
pp. 6310-6313 ◽  
Author(s):  
Alexander G. Ekström ◽  
Van Kelly ◽  
Jon Marles-Wright ◽  
Scott L. Cockroft ◽  
Dominic J. Campopiano
Keyword(s):  
Mass Spectrometry ◽  
Reaction Mechanism ◽  
Active Site ◽  
Covalent Modification ◽  
Elimination Reaction ◽  
Covalent Adduct ◽  
Michael Type Addition

Mass spectrometry and modelling shows the antimicrobial inhibitor 4,5-dichloro-1,2-dithiol-3-one (HR45) acts by forming a covalent adduct with the target β-ketoacyl-ACP synthase III (FabH). The 5-chloro substituent directs attack of the essential active site thiol (C112) via a Michael type addition elimination reaction mechanism.

CH3-ReO3 on γ-Al2O3: Activity, selectivity, active site and deactivation in olefin metathesis

2008 ◽  
Vol 253 (1) ◽  
pp. 180-190 ◽  
Author(s):  
A SALAMEH ◽  
A BAUDOUIN ◽  
D SOULIVONG ◽  
V BOEHM ◽  
M ROEPER ◽  
...  
Keyword(s):  
Active Site ◽  
Olefin Metathesis

scholarly journals Proton–Electron Transfer to the Active Site Is Essential for the Reaction Mechanism of Soluble Δ9-Desaturase

2020 ◽  
Vol 142 (23) ◽  
pp. 10412-10423 ◽  
Author(s):  
Daniel Bím ◽  
Jakub Chalupský ◽  
Martin Culka ◽  
Edward I. Solomon ◽  
Lubomír Rulíšek ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Reaction Mechanism ◽  
Active Site ◽  
Δ9 Desaturase

Insight into the active site and reaction mechanism for selective oxidation of methane to methanol using H2O2 on a Rh1/ZrO2 catalyst

2020 ◽  
Vol 44 (4) ◽  
pp. 1632-1639 ◽  
Author(s):  
Qi Zhao ◽  
Bing Liu ◽  
Yuebing Xu ◽  
Feng Jiang ◽  
Xiaohao Liu
Keyword(s):  
Reaction Mechanism ◽  
Selective Oxidation ◽  
Active Site ◽  
Oxidation Of Methane ◽  
Methanol Formation ◽  
Zro2 Catalyst ◽  
Insight Into

Five-coordinated Rh leads to the over-oxidation of CH4, while four-coordinated Rh stabilizes CH3 and facilitates methanol formation via the CH3OOH intermediate.

scholarly journals The metal centres of particulate methane mono-oxygenase

2008 ◽  
Vol 36 (6) ◽  
pp. 1134-1137 ◽  
Author(s):  
Amy C. Rosenzweig
Keyword(s):  
Crystal Structure ◽  
Reaction Mechanism ◽  
Structure Determination ◽  
Active Site ◽  
Spectroscopic Data ◽  
Present Review ◽  
Methylococcus Capsulatus ◽  
Research Groups ◽  
Oxidation Of Methane ◽  
Before And After

pMMO (particulate methane mono-oxygenase) is an integral membrane metalloenzyme that catalyses the oxidation of methane to methanol. The pMMO metal active site has not been identified, precluding detailed investigation of the reaction mechanism. Models for the metal centres proposed by various research groups have evolved as crystallographic and spectroscopic data have become available. The present review traces the evolution of these active-site models before and after the 2005 Methylococcus capsulatus (Bath) pMMO crystal structure determination.

Sign in / Sign up

Export Citation Format

Share Document