scholarly journals Determination of interproton distances from NOESY spectra in the active site of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase

1993 ◽  
Vol 115 (12) ◽  
pp. 5237-5245 ◽  
Author(s):  
Marco Sette ◽  
Jeffrey S. De Ropp ◽  
Griselda Hernandez ◽  
Gerd N. La Mar
Keyword(s):  
Horseradish Peroxidase ◽  
Active Site ◽  
Noesy Spectra ◽  
Interproton Distances

Statistical Description of Isotope Exchange Processes: A Multisite Model for the 18O Exchange

1982 ◽  
Vol 37 (11-12) ◽  
pp. 1161-1169 ◽  
Author(s):  
Paul Rösch
Keyword(s):  
Active Site ◽  
Isotope Exchange ◽  
Analytical Procedure ◽  
Matrix Formalism ◽  
Model Calculations ◽  
Exchange Processes ◽  
Reaction Solution ◽  
Different Types ◽  
Refinement Procedure

Abstract An analytical procedure has been developed for the determination of isotope exchange processes as exemplified by the 18O exchange catalysed by enzyme-nucleotide complexes. The model is able to handle more than one type of active site per reaction solution and is also able to distinguish between different types of inequivalence of the oxygens of enzyme bound Pi. Use of transition matrix formalism and basic statistical considerations lead directly to the simple model. A data refinement procedure is introduced and model calculations are shown.

Nonlinear Vibrations in a 2-Dimensional Protein Cluster Model with Linear Bonds

2000 ◽  
Vol 214 (1) ◽  
Author(s):  
E.G. Shidlovskaya ◽  
L. Schimansky-Geier ◽  
Yu.M. Romanovsky
Keyword(s):  
Active Site ◽  
Internal Resonance ◽  
Cluster Model ◽  
Active Sites ◽  
Nonlinear Vibrations ◽  
Nonlinear Phenomena ◽  
Two Dimensional ◽  
Dimensional Model ◽  
Two Dimensional Model

A two dimensional model for the substrate inside a pocket of an active site of an enzyme is presented and investigated as a vibrational system. The parameters of the system are evaluated for α-chymotrypsin. In the case of internal resonance it is analytically and numerically shown that the energy concentrated on a certain degree of freedom might be several times larger than in the non-resonant case. Additionally, the system is driven by harmonic excitations and again energy due to nonlinear phenomena is redistributed inhomogeneously. These results may be of importance for the determination of the rates of catalytic events of substrates bound in pockets of active sites.

Potentiometric determination of ionizations at the active site of papain

Biochemistry ◽  
1976 ◽  
Vol 15 (23) ◽  
pp. 5009-5017 ◽  
Author(s):  
Sidney D. Lewis ◽  
Frederick A. Johnson ◽  
Jules A. Shafer
Keyword(s):  
Active Site ◽  
Potentiometric Determination
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