Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of .beta.-methylaspartate to glutamate

Biochemistry ◽  
1972 ◽  
Vol 11 (2) ◽  
pp. 253-264 ◽  
Author(s):  
R. G. Eagar ◽  
B. G. Baltimore ◽  
M. M. Herbst ◽  
H. A. Barker ◽  
J. H. Richards
Keyword(s):  
Mechanism Of Action ◽  
Hydrogen Transfer ◽  
Coenzyme B12

scholarly journals Studies on the Mechanism of Action of Coenzyme B12

1972 ◽  
Vol 247 (13) ◽  
pp. 4197-4207
Author(s):  
Thomas H. Finlay ◽  
Jay Valinsky ◽  
Kazuyoshi Sato ◽  
Robert H. Abeles
Keyword(s):  
Mechanism Of Action ◽  
Coenzyme B12

The mechanism of action of coenzyme B12

Vitamin B12 ◽  
1979 ◽  
pp. 575-586
Author(s):  
D. Dolphin ◽  
A. R. Banks ◽  
W. R. Cullen ◽  
A. R. Cutler ◽  
R. B. Silverman
Keyword(s):  
Mechanism Of Action ◽  
Coenzyme B12

Insights into the mechanisms of adenosylcobalamin (coenzyme B12)-dependent enzymes from rapid chemical quench experiments

2009 ◽  
Vol 37 (2) ◽  
pp. 336-342 ◽  
Author(s):  
E. Neil G. Marsh
Keyword(s):  
Free Radicals ◽  
Steady State ◽  
Kinetic Isotope Effect ◽  
Hydrogen Transfer ◽  
Coenzyme B12 ◽  
Hydrogen Atoms ◽  
Glutamate Mutase ◽  
Kinetic Isotope ◽  
Steady State Kinetic ◽  
State Kinetic

Glutamate mutase is one of a group of adenosylcobalamin-dependent enzymes that use free radicals to catalyse unusual and chemically difficult rearrangements involving 1,2-migrations of hydrogen atoms. A key mechanistic feature of these enzymes is the transfer of the migrating hydrogen atom between substrate, coenzyme and product. The present review summarizes recent experiments from my laboratory that have used rapid chemical quench techniques to identify intermediates in the reaction and probe the mechanism of hydrogen transfer through a variety of pre-steady-state kinetic isotope effect measurements.

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