Photolytic Cleavage of Co–C Bond in Coenzyme B12-Dependent Glutamate Mutase

2019 ◽  
Vol 123 (12) ◽  
pp. 2585-2598 ◽  
Author(s):  
Abdullah Al Mamun ◽  
Megan J. Toda ◽  
Piotr Lodowski ◽  
Pawel M. Kozlowski
Keyword(s):  
Coenzyme B12 ◽  
Glutamate Mutase

Coenzyme B12 dependent glutamate mutase

2002 ◽  
Vol 6 (5) ◽  
pp. 598-603 ◽  
Author(s):  
Karl Gruber ◽  
Christoph Kratky
Keyword(s):  
Coenzyme B12 ◽  
Glutamate Mutase

Protein–coenzyme interactions in adenosylcobalamin-dependent glutamate mutase

2001 ◽  
Vol 355 (1) ◽  
pp. 131-137 ◽  
Author(s):  
Marja S. HUHTA ◽  
Hao-Ping CHEN ◽  
Craig HEMANN ◽  
C. Russ HILLE ◽  
E. Neil G. MARSH
Keyword(s):  
Gel Filtration ◽  
Visible Spectrum ◽  
Titration Calorimetry ◽  
Coenzyme B12 ◽  
Glutamate Mutase ◽  
Carbon Bond ◽  
Coenzyme Binding ◽  
Radical Intermediates ◽  
Bond Stretching ◽  
Uv Visible

Glutamate mutase catalyses an unusual isomerization involving free-radical intermediates that are generated by homolysis of the cobalt–carbon bond of the coenzyme adenosylcobalamin (coenzyme B12). A variety of techniques have been used to examine the interaction between the protein and adenosylcobalamin, and between the protein and the products of coenzyme homolysis, cob(II)alamin and 5′-deoxyadenosine. These include equilibrium gel filtration, isothermal titration calorimetry, and resonance Raman, UV-visible and EPR spectroscopies. The thermodynamics of adenosylcobalamin binding to the protein have been examined and appear to be entirely entropy-driven, with ∆S = 109 Jċmol-1ċK-1. The cobalt–carbon bond stretching frequency is unchanged upon coenzyme binding to the protein, arguing against a ground-state destabilization of the cobalt–carbon bond of adenosylcobalamin by the protein. However, reconstitution of the enzyme with cob(II)alamin and 5′-deoxyadenosine, the two stable intermediates formed subsequent to homolysis, results in the blue-shifting of two of the bands comprising the UV-visible spectrum of the corrin ring. The most plausible interpretation of this result is that an interaction between the protein, 5′-deoxyadenosine and cob(II)alamin introduces a distortion into the ring corrin that perturbs its electronic properties.

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.

Identification of the 4-Glutamyl Radical as an Intermediate in the Carbon Skeleton Rearrangement Catalyzed by Coenzyme B12-Dependent Glutamate Mutase fromClostridiumcochlearium†

Biochemistry ◽  
1998 ◽  
Vol 37 (12) ◽  
pp. 4105-4113 ◽  
Author(s):  
Harald Bothe ◽  
Daniel J. Darley ◽  
Simon P. J. Albracht ◽  
Gary J. Gerfen ◽  
Bernard T. Golding ◽  
...  
Keyword(s):  
Carbon Skeleton ◽  
Coenzyme B12 ◽  
Glutamate Mutase

EXAFS Data Indicate a “Normal” Axial Cobalt−Nitrogen Bond of the Organo-B12Cofactor in the Two Coenzyme B12-Dependent Enzymes Glutamate Mutase and 2-Methyleneglutarate Mutase

1999 ◽  
Vol 121 (50) ◽  
pp. 11780-11789 ◽  
Author(s):  
Frederic Champloy ◽  
Gerwald Jogl ◽  
Riikka Reitzer ◽  
Wolfgang Buckel ◽  
Harald Bothe ◽  
...  
Keyword(s):  
Coenzyme B12 ◽  
Glutamate Mutase ◽  
Exafs Data ◽  
Nitrogen Bond
Sign in / Sign up

Export Citation Format

Share Document