2D NMR assignment of hyperfine-shifted resonances in strongly paramagnetic metalloproteins: resting-state horseradish peroxidase

1991 ◽  
Vol 113 (11) ◽  
pp. 4348-4350 ◽  
Author(s):  
Jeffrey S. De Ropp ◽  
Gerd N. La Mar
Keyword(s):  
Horseradish Peroxidase ◽  
Resting State ◽  
Nmr Assignment ◽  
2D Nmr

2D NMR of paramagnetic metalloenzymes: Cyanide-inhibited horseradish peroxidase

1991 ◽  
Vol 1 (2) ◽  
pp. 175-190 ◽  
Author(s):  
Jeffrey S. de Ropp ◽  
Liping P. Yu ◽  
Gerd N. La Mar
Keyword(s):  
Horseradish Peroxidase ◽  
2D Nmr

scholarly journals Complete 2D NMR assignment and antifungal activity of ishwarane isolated from Hortonia, a genus endemic to Sri Lanka

2008 ◽  
Vol 36 (1) ◽  
pp. 109 ◽  
Author(s):  
Rukmal Ratnayake ◽  
Susanthi Jayasinghe ◽  
BM Ratnayake Bandara ◽  
Raymond J Andersen ◽  
Veranja Karunaratne
Keyword(s):  
Antifungal Activity ◽  
Sri Lanka ◽  
Nmr Assignment ◽  
2D Nmr

(-)-Armepavine: Gradient-Enhanced 2D NMR Study and X-Ray Crystal Structure Determination

1997 ◽  
Vol 62 (10) ◽  
pp. 1623-1630 ◽  
Author(s):  
Radek Marek ◽  
Jaromír Marek ◽  
Jiří Dostál ◽  
Jiří Slavík
Keyword(s):  
Crystal Structure ◽  
Nmr Spectroscopy ◽  
Structure Determination ◽  
Nmr Assignment ◽  
2D Nmr ◽  
X Ray Diffraction ◽  
2D Nmr Spectroscopy ◽  
X Ray ◽  
Nmr Study ◽  
Benzylisoquinoline Alkaloid

(-)-Armepavine, a benzylisoquinoline alkaloid isolated from Papaver caucasicum, was examined by gradient-enhanced 2D NMR spectroscopy and X-ray diffraction analysis. Unambiguous 1H, 13C, and 15N NMR assignment of the title alkaloid is reported.

ChemInform Abstract: Complete 1H and 13C NMR Assignment of Balearone by 2D NMR Spectroscopy.

ChemInform ◽  
2010 ◽  
Vol 22 (52) ◽  
pp. no-no
Author(s):  
V. AMICO ◽  
M. PIATTELLI ◽  
P. NERI ◽  
M. RECUPERO
Keyword(s):  
Nmr Spectroscopy ◽  
13C Nmr ◽  
Nmr Assignment ◽  
2D Nmr ◽  
2D Nmr Spectroscopy ◽  
1H And 13C Nmr

Oxidation of 4-tert-Butylcatechol and Dopamine by Hydrogen Peroxide Catalysed by Horseradisch Peroxidase

1999 ◽  
Vol 380 (6) ◽  
Author(s):  
M. García-Moreno ◽  
M. Moreno-Conesa ◽  
J.N. Rodríguez-López ◽  
F. García-Cánovas ◽  
R. Varón
Keyword(s):  
Hydrogen Peroxide ◽  
Electron Transfer ◽  
Horseradish Peroxidase ◽  
Resting State ◽  
Intermediate Compound ◽  
Transfer Reactions ◽  
Single Electron Transfer ◽  
Compound I ◽  
Compound Ii ◽  
Enzyme Intermediate

AbstractThe catalytic cycle of horseradish peroxidase (HRP; donor:hydrogen peroxide oxidoreductase; EC 1.11.1.7) is initiated by a rapid oxidation of it by hydrogen peroxide to give an enzyme intermediate, compound I, which reverts to the resting state via two successive single electron transfer reactions from reducing substrate molecules, the first yielding a second enzyme intermediate, compound II. To investigate the mechanism of action of horseradish peroxidase on catechol substrates we have studied the oxidation of both 4-

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