Pre-Steady-State Kinetic Investigation of Intermediates in the Reaction Catalyzed by Adenosylcobalamin-Dependent Glutamate Mutase†

Biochemistry ◽  
1999 ◽  
Vol 38 (41) ◽  
pp. 13684-13691 ◽  
Author(s):  
Hung-Wei Chih ◽  
E. Neil G. Marsh
Keyword(s):  
Steady State ◽  
Kinetic Investigation ◽  
Glutamate Mutase ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Pre-steady-state kinetic investigation of bypass of a bulky guanine lesion by human Y-family DNA polymerases

DNA Repair ◽  
2016 ◽  
Vol 46 ◽  
pp. 20-28 ◽  
Author(s):  
E. John Tokarsky ◽  
Varun V. Gadkari ◽  
Walter J. Zahurancik ◽  
Chanchal K. Malik ◽  
Ashis K. Basu ◽  
...  
Keyword(s):  
Steady State ◽  
Dna Polymerases ◽  
Kinetic Investigation ◽  
Steady State Kinetic ◽  
Y Family ◽  
State Kinetic

Pre-Steady-State Kinetic Studies on the Glu171Gln Active Site Mutant of Adenosylcobalamin-Dependent Glutamate Mutase†

Biochemistry ◽  
2002 ◽  
Vol 41 (52) ◽  
pp. 15803-15809 ◽  
Author(s):  
Prashanti Madhavapeddi ◽  
David P. Ballou ◽  
E. Neil G. Marsh
Keyword(s):  
Steady State ◽  
Active Site ◽  
Kinetic Studies ◽  
Glutamate Mutase ◽  
Steady State Kinetic ◽  
State Kinetic

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.

Steady-State Kinetic Investigation of Cytochrome P450cam:  Interaction with Redox Partners and Reaction with Molecular Oxygen†

Biochemistry ◽  
2004 ◽  
Vol 43 (1) ◽  
pp. 271-281 ◽  
Author(s):  
Matthew M. Purdy ◽  
Laura S. Koo ◽  
Paul R. Ortiz de Montellano ◽  
Judith P. Klinman
Keyword(s):  
Steady State ◽  
Molecular Oxygen ◽  
Kinetic Investigation ◽  
Cytochrome P450cam ◽  
Redox Partners ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Thermodynamic and steady-state-kinetic investigation of the effect of NN′-dicyclohexylcarbodi-imide on H+ translocation by the mitochondrial cytochrome bc1 complex

1985 ◽  
Vol 225 (2) ◽  
pp. 407-411 ◽  
Author(s):  
M D Brand ◽  
M K Al-Shawi ◽  
G C Brown ◽  
B D Price
Keyword(s):  
Steady State ◽  
Thermodynamic Assessment ◽  
Cytochrome Bc1 ◽  
Kinetic Investigation ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Kinetic Measurements ◽  
Steady State Kinetic ◽  
Force Ratio ◽  
State Kinetic

Steady-state kinetic measurements showed that NN′-dicyclohexylcarbodi-imide decreased the observed H+/2e ratio of H+ transport by mitochondria respiring on succinate, acting mainly at the cytochrome bc1 complex. Thermodynamic assessment of the H+/2e ratio by measuring the force ratio across the bc1 complex showed that the inhibitor did not affect H+ translocation. Possible explanations of this disagreement between methods are examined; we conclude that the inhibitor does not alter the mechanistic stoichiometry of H+ pumping by the bc1 complex.

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