scholarly journals Analysis of Reaction Mechanism of Inverting Cellulase Including a Proton Pathway by a Joint Analysis of Neutron/X-ray Crystallography

hamon ◽  
2016 ◽  
Vol 26 (3) ◽  
pp. 139-142
Author(s):  
Akihiko Nakamura ◽  
Takuya Ishida ◽  
Katsuhiro Kusaka ◽  
Ichiro Tanaka ◽  
Nobuo Niimura ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Joint Analysis ◽  
X Ray ◽  
X Ray Crystallography

scholarly journals Reaction Mechanism Based on X-ray Crystallography at Atomic Resolution of Endopolygalacutronase I from Fungus Stereum purpureum

2004 ◽  
Vol 51 (2) ◽  
pp. 161-167 ◽  
Author(s):  
Tetsuya Shimizu ◽  
Toru Nakatsu ◽  
Kazuo Miyairi ◽  
Toshikatsu Okuno ◽  
Hiroaki Kato
Keyword(s):  
Reaction Mechanism ◽  
Atomic Resolution ◽  
X Ray ◽  
X Ray Crystallography

scholarly journals Reaction mechanism of the bioluminescent protein mnemiopsin1 revealed by X-ray crystallography and QM/MM simulations

2018 ◽  
Vol 294 (1) ◽  
pp. 20-27 ◽  
Author(s):  
Maryam Molakarimi ◽  
Michael A. Gorman ◽  
Ammar Mohseni ◽  
Zaiddodine Pashandi ◽  
Majid Taghdir ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
X Ray ◽  
X Ray Crystallography ◽  
Bioluminescent Protein

scholarly journals Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism

2005 ◽  
Vol 386 (10) ◽  
pp. 999-1006 ◽  
Author(s):  
Matthias Boll ◽  
Bernhard Schink ◽  
Albrecht Messerschmidt ◽  
Peter M.H. Kroneck
Keyword(s):  
Reaction Mechanism ◽  
Structural Analysis ◽  
Triple Bond ◽  
Three Dimensional ◽  
Reaction Centers ◽  
Dimensional Structure ◽  
X Ray ◽  
X Ray Crystallography ◽  
Coa Reductase ◽  
Tungsten Enzymes

Abstract The molybdenum enzymes 4-hydroxybenzoyl-CoA reductase and pyrogallol-phloroglucinol transhydroxylase and the tungsten enzyme acetylene hydratase catalyze reductive dehydroxylation reactions, i.e., transhydroxylation between phenolic residues and the addition of water to a triple bond. Such activities are unusual for this class of enzymes, which carry either a mononuclear Mo or W center. Crystallization and subsequent structural analysis by high-resolution X-ray crystallography has helped to resolve the reaction centers of these enzymes to a degree that allows us to understand the interaction of the enzyme and the respective substrate(s) in detail, and to develop a concept for the respective reaction mechanism, at least in two cases.

Reaction Mechanism ofEscherichia coliDihydrodipicolinate Synthase Investigated by X-ray Crystallography and NMR Spectroscopy†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (1) ◽  
pp. 24-33 ◽  
Author(s):  
Stefan Blickling ◽  
Christian Renner ◽  
Bernd Laber ◽  
Hans-Dieter Pohlenz ◽  
Tad A. Holak ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Nmr Spectroscopy ◽  
X Ray ◽  
X Ray Crystallography

scholarly journals Reaction of Dialumane Incorporating Bulky Eind Groups with Pyridines

Inorganics ◽  
2019 ◽  
Vol 7 (11) ◽  
pp. 129
Author(s):  
Murosaki ◽  
Ohno ◽  
Agou ◽  
Hashizume ◽  
Matsuo
Keyword(s):  
Reaction Mechanism ◽  
Nmr Spectroscopy ◽  
Lewis Base ◽  
Organoaluminum Compounds ◽  
Similar Reaction ◽  
Deuterium Labeling ◽  
X Ray ◽  
X Ray Crystallography

The reaction of the bulky Eind-based dialumane, (Eind)HAl(μ-H)2AlH(Eind) (1) (Eind = 1,1,3,3,5,5,7,7-octaethyl-s-hydrindacen-4-yl), with pyridines is described. When 1 was treated with pyridine (Py) in toluene, the Py adduct of aryldihydroalumane, Py→AlH2(Eind) (2), was initially formed. Then, the hydroalumination of Py took place to yield the Py-bound aryl(1,4-dihydropyrid-1-yl)hydroalumane, Py→AlH(1,4-dihydropyrid-1-yl)(Eind) (3). A similar reaction with a stronger Lewis base, 4-pyrrolidinopyridine (PPy), produced the stable PPy adduct, PPy→AlH2(Eind) (4). The resulting organoaluminum compounds have been fully characterized by NMR spectroscopy as well as X-ray crystallography. The reaction mechanism from 1 to 3 via 2 has been examined by deuterium labeling experiments using (Eind)DAl(μ-D)2AlD(Eind) (1-d4).

scholarly journals Reaction Mechanism of Glutamate Carboxypeptidase II Revealed by Mutagenesis, X-ray Crystallography, and Computational Methods

Biochemistry ◽  
2009 ◽  
Vol 48 (19) ◽  
pp. 4126-4138 ◽  
Author(s):  
Vojtěch Klusák ◽  
Cyril Bařinka ◽  
Anna Plechanovová ◽  
Petra Mlčochová ◽  
Jan Konvalinka ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Computational Methods ◽  
Glutamate Carboxypeptidase Ii ◽  
X Ray ◽  
X Ray Crystallography ◽  
Glutamate Carboxypeptidase
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