Theoretical analysis of cyclic reaction mechanisms of two ethylenes

2002 ◽  
Vol 90 (2) ◽  
pp. 549-554 ◽  
Author(s):  
Shogo Sakai
2009 ◽  
Vol 113 (43) ◽  
pp. 11758-11762 ◽  
Author(s):  
José J. Plata ◽  
Mónica García-Mota ◽  
Ataualpa A. C. Braga ◽  
Núria López ◽  
Feliu Maseras

2009 ◽  
Vol 127 (1-2) ◽  
pp. 95-108 ◽  
Author(s):  
Ana Arenillas ◽  
Borja Arias ◽  
Fernando Rubiera ◽  
José J. Pis ◽  
Ramón López ◽  
...  

1994 ◽  
Vol 15 (5) ◽  
pp. 479-487 ◽  
Author(s):  
X. Assfeld ◽  
M. F. Ruiz-lopez ◽  
J. Gonzalez ◽  
R. Lopez ◽  
J. A. Sordo ◽  
...  

Author(s):  
A. Gómez ◽  
P. Schabes-Retchkiman ◽  
M. José-Yacamán ◽  
T. Ocaña

The splitting effect that is observed in microdiffraction pat-terns of small metallic particles in the size range 50-500 Å can be understood using the dynamical theory of electron diffraction for the case of a crystal containing a finite wedge. For the experimental data we refer to part I of this work in these proceedings.


Author(s):  
Jeff Gelles

Mechanoenzymes are enzymes which use a chemical reaction to power directed movement along biological polymer. Such enzymes include the cytoskeletal motors (e.g., myosins, dyneins, and kinesins) as well as nucleic acid polymerases and helicases. A single catalytic turnover of a mechanoenzyme moves the enzyme molecule along the polymer a distance on the order of 10−9 m We have developed light microscope and digital image processing methods to detect and measure nanometer-scale motions driven by single mechanoenzyme molecules. These techniques enable one to monitor the occurrence of single reaction steps and to measure the lifetimes of reaction intermediates in individual enzyme molecules. This information can be used to elucidate reaction mechanisms and determine microscopic rate constants. Such an approach circumvents difficulties encountered in the use of traditional transient-state kinetics techniques to examine mechanoenzyme reaction mechanisms.


Author(s):  
A. Angel ◽  
K. Miller ◽  
V. Seybold ◽  
R. Kriebel

Localization of specific substances at the ultrastructural level is dependent on the introduction of chemicals which will complex and impart an electron density at specific reaction sites. Peroxidase-antiperoxidase(PAP) methods have been successfully applied at the electron microscopic level. The PAP complex is localized by addition of its substrate, hydrogen peroxide and an electron donor, usually diaminobenzidine(DAB). On oxidation, DAB forms an insoluble polymer which is able to chelate with osmium tetroxide becoming electron dense. Since verification of reactivity is visual, discrimination of reaction product from osmiophillic structures may be difficult. Recently, x-ray microanalysis has been applied to examine cytochemical reaction precipitates, their distribution in tissues, and to study cytochemical reaction mechanisms. For example, immunoreactive sites labelled with gold have been ascertained by means of x-ray microanalysis.


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