On the relationship between the structures of Cu(II) complexes and their chemical transformations

1983 ◽  
Vol 26 (1) ◽  
pp. 95-100 ◽  
Author(s):  
H. Langfelderová ◽  
V. Karla ◽  
M. Lirkešová ◽  
J. Gažo
Keyword(s):  
Chemical Transformations ◽  
The Relationship

On the relationship between the structures of Cu(II) complexes and their chemical transformations

1979 ◽  
Vol 17 (1) ◽  
pp. 107-114 ◽  
Author(s):  
H. Langfelderová ◽  
M. Linkešová ◽  
M. Serátor ◽  
J. GaŽo
Keyword(s):  
Chemical Transformations ◽  
The Relationship

The relationship between the structures of Cu(II) complexes and their chemical transformations: VII

1986 ◽  
Vol 31 (5) ◽  
pp. 1143-1151
Author(s):  
H. Langfelderová ◽  
L'. Macášková ◽  
K. Otrubová ◽  
J. Gažo
Keyword(s):  
Chemical Transformations ◽  
The Relationship

On the relationship between the structures of Cu(II) complexes and their chemical transformations IX

1989 ◽  
Vol 35 (3) ◽  
pp. 857-866 ◽  
Author(s):  
H. Langfelderová ◽  
M. Linkešová ◽  
P. Ambrovič ◽  
A. Riedlmajerová
Keyword(s):  
Chemical Transformations ◽  
The Relationship

Probing coupled motions in enzymatic hydrogen tunnelling reactions

2009 ◽  
Vol 37 (2) ◽  
pp. 349-353 ◽  
Author(s):  
Rudolf K. Allemann ◽  
Rhiannon M. Evans ◽  
E. Joel Loveridge
Keyword(s):  
Protein Dynamics ◽  
Dihydrofolate Reductase ◽  
Thermotoga Maritima ◽  
Quantum Mechanical ◽  
Extreme Conditions ◽  
Chemical Transformations ◽  
Complex Reaction ◽  
Detailed Mechanism ◽  
The Relationship ◽  
Catalytic Power

Much work has gone into understanding the physical basis of the enormous catalytic power of enzymes over the last 50 years or so. Nevertheless, the detailed mechanism used by Nature's catalysts to speed chemical transformations remains elusive. DHFR (dihydrofolate reductase) has served as a paradigm to study the relationship between the structure, function and dynamics of enzymatic transformations. A complex reaction cascade, which involves rearrangements and movements of loops and domains of the enzyme, is used to orientate cofactor and substrate in a reactive configuration from which hydride is transferred by quantum mechanical tunnelling. In the present paper, we review results from experiments that probe the influence of protein dynamics on the chemical step of the reaction catalysed by TmDHFR (DHFR from Thermotoga maritima). This enzyme appears to have evolved an optimal structure that can maintain a catalytically competent conformation under extreme conditions.

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