Pre-Steady-State Measurement of Intrinsic Secondary Tritium Isotope Effects Associated with the Homolysis of Adenosylcobalamin and the Formation of 5′-Deoxyadensosine in Glutamate Mutase

Biochemistry

Volumn 43, Issue 8, 2004, Pages 2155-2158

  Cheng, Mou Chi ^a   Marsh, E Neil G ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; COENZYMES; ENZYME KINETICS; ISOTOPES;

HOMOLYSIS; TRANSITION STATES;

BIOCHEMISTRY;

5' DEOXYADENOSINE; CARBON; COBALT; COBAMAMIDE; DEOXYADENOSINE; GLUTAMATE SYNTHASE; GLUTAMIC ACID; HYDROGEN; ISOTOPE; METHYLASPARTATE MUTASE; MUTASE; TRITIUM; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL BOND; COENZYME; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; HYBRIDIZATION; NONPHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; REACTION ANALYSIS; STEADY STATE;

BINDING, COMPETITIVE; CATALYSIS; COBAMIDES; DEOXYADENOSINES; ENZYME STABILITY; GLUTAMIC ACID; HOLOENZYMES; HYDROGEN BONDING; HYDROLYSIS; INTRAMOLECULAR TRANSFERASES; KINETICS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TRITIUM;

TRITIUM;

EID: 1442276496     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036122w     Document Type: Article

References (27)

1. Marsh, E. N. G., and Drennan, C. L. (2001) Adenosylcobalamin-dependent isomerases: new insights into structure and mechanism, Curr. Opin. Chem. Biol. 5, 499-505.
2. Frey, P. A. (2001) Radical mechanisms of enzymatic catalysis, Annu. Rev. Biochem. 70, 121-148.
3. 12-Dependent Enzymes, Biochemistry 40, 6191-6198.
4. 12-dependent glutamate mutase, Bioorg. Chem. 28, 176-189.
5. Banerjee, R. (1997) The yin-yang of cobalamin biochemistry, Chem. Biol. 4, 175-186.
6. Marsh, E. N. G., and Ballou, D. P. (1998) Coupling of cobalt-carbon bond homolysis and hydrogen atom abstraction in adenosylcobalamin-dependent glutamate mutase, Biochemistry 37, 11864-11872.
7. Licht, S. S., Lawrence, C. C., and Stubbe, J. (1999) Thermodynamic and kinetic studies on cobalt-carbon bond homolysis by ribonucleotide triphosphate reductase: the importance of entropy in catalysis, Biochemistry 34, 1234-1242.
8. Padmakumar, R., and Banerjee, R. (1997) Evidence that cobalt-carbon bond homolysis is coupled to hydrogen atom abstraction from substrate in methylmalonyl-CoA mutase, Biochemistry 36, 3713-3718.
9. Bandarian, V., and Reed, G. H. (2000) Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: Determination of the number of exchangeable hydrogens in the enzyme-cofactor complex, Biochemistry 39, 12069-12075.
10. Licht, S. S., Booker, S., and Stubbe, J. A. (1999) Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: Evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation, Biochemistry 38, 1221-1233.
11. Chen, D. W., Abend, A., Stubbe, J., and Frey, P. A. (2003) Epimerization at carbon-5′ of (5′R)-[5′,H-2]adenosylcobalamin by ribonucleoside triphosphate reductase: Cysteine 408-independent cleavage of the Co-C5′ bond, Biochemistry 42, 4578-4584.
12. Chowdhury, S., and Banerjee, R. (2000) Evidence for quantum mechanical tunneling in the coupled cobalt-carbon bond homolysis-substrate radical generation reaction catalyzed by methylmalonyl-CoA mutase, J. Am. Chem. Soc. 122, 5417-5418.
13. Bahnson, B. J., and Klinman, J. P. (1995) Methods Enzymol. (Enzyme Kinet, Mech, Part D) 249, 373-397.
14. Cook, P. F., Oppenheimer, N. J., and Cleland, W. W. (1981) Secondary deuterium and nitrogen-15 isotope effects in enzyme catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase, Biochemistry 20, 1817-1825.
15. Hermes, J. D., and Cleland, W. W. (1984) Evidence from multiple isotope effect determinations for coupled hydrogen motion and tunneling in the reaction catalyzed by glucose-6-phosphate-dehydrogenase, J. Am. Chem. Soc. 106, 7263-7264.
16. Schramm, V. L. (2001) Transition state variation in enzymatic reactions, Curr. Opin. Chem. Biol. 5, 556-563.
17. Chen, X. Y., Berti, P. J., and Schramm, V. L. (2000) Transition-state analysis for depurination of DNA by ricin A-chain, J. Am. Chem. Soc. 122, 6527-6534.
18. Suhnel, J., and Schowen, R. L. (1991) in Enzyme mechanism from isotope effects (Cook, P. F., Ed.) pp 3-35, CRC Press, Boca Raton, FL.
19. Chen, H. P., and Marsh, E. N. G. (1997) Adenosylcobalamin-dependent glutamate mutase: examination of substrate and coenzyme binding in an engineered fusion protein possessing simplified subunit structure and kinetic properties, Biochemistry 36, 14939-45.
20. Marsh, E. N. G. (1995) Tritium isotope effects in adenosylcobalamin-dependent glutamate mutase: implications for the mechanism, Biochemistry 34, 7542-7547.
21. Brown, K, L., Cheng, S., Zou, X., Li, J., Chen, G. D., Valente, E. J., Zubkowski, J. D., and Marques, H. M. (1998) Structural and enzymatic studies of a new analogue of coenzyme B-12 with an alpha-adenosyl upper axial ligand, Biochemistry 37, 9704-9715.
22. Chih, H. W., and Marsh, E. N. G. (1999) Pre-steady-state kinetic investigation of intermediates in the reaction catalyzed by adenosylcobalamin-dependent glutamate mutase, Biochemistry 38, 13684-13691.
23. Chih, H.-W., and Marsh, E. N. G. (2001) Tritium partitioning and isotope effects in adenosylcobalamin-dependent glutamate mutase, Biochemistry 40, 13060-13067.
24. Doll, K. M., Bender, B. R., and Finke, R. G. (2003) The first experimental test of the hypothesis that enzymes have evolved to enhance hydrogen tunneling, J. Am. Chem. Soc. 125, 10877-10884.
25. Dong, S. L., Padmakumar, R., Banerjee, R., and Spiro, T. G. (1998) Co-C force constants from resonance Raman spectra of alkylcobalamins: insensitivity to dimethylbenzylimidazole coordination, Inorg. Chim. Acta 270, 392-398.
26. Marques, H. M., and Brown, K. L. (2002) Molecular mechanics and molecular dynamics simulations of porphyrins, metalloporphyrins, heme proteins and cobalt corrinoids, Coord. Chem. Rev. 225, 123-158.
27. Marques, H. M., and Brown, K. L. (1999) The structure of cobalt corrinoids based on molecular mechanics and NOE-restrained molecular mechanics and dynamics simulations, Coord. Chem. Rev. 192, 127-153.