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Volumn 44, Issue 9, 2005, Pages 3153-3158

Characterization of a succinyl-CoA radical-Cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; COMPUTER SIMULATION; DEUTERIUM; ELECTRON SPIN RESONANCE SPECTROSCOPY; SUBSTITUTION REACTIONS;

EID: 14644401110     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0482102     Document Type: Article
Times cited : (36)

References (32)
  • 1
    • 0035967504 scopus 로고    scopus 로고
    • 12-dependent enzymes
    • 12-dependent enzymes, Biochemistry 40, 6191-6198.
    • (2001) Biochemistry , vol.40 , pp. 6191-6198
    • Banerjee, R.1
  • 2
    • 0037899473 scopus 로고    scopus 로고
    • 12-dependent mutases
    • 12-dependent mutases, Chem. Rev. 103, 2083-2094.
    • (2003) Chem. Rev. , vol.103 , pp. 2083-2094
    • Banerjee, R.1
  • 5
    • 0016244339 scopus 로고
    • 12-dependent Enzyme. The participation of paramagnetic species in the catalytic deamination of 2-aminopropanol
    • 12- dependent Enzyme. The participation of paramagnetic species in the catalytic deamination of 2-aminopropanol, J. Biol. Chem. 249, 4537-4544.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4537-4544
    • Babior, B.M.1    Moss, T.H.2    Orme-Johnson, W.H.3    Beinert, H.4
  • 6
    • 33748218119 scopus 로고
    • 12-dependent methylmalonyl-CoA mutase reaction shown by ESR spectroscopy
    • 12-dependent methylmalonyl-CoA mutase reaction shown by ESR spectroscopy, Angew. Chem., Int. Ed. Engl. 31, 215-216.
    • (1992) Angew. Chem., Int. Ed. Engl. , vol.31 , pp. 215-216
    • Zhao, Y.1    Such, P.2    Retey, J.3
  • 7
    • 0001462145 scopus 로고    scopus 로고
    • Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium
    • Bothe, H., Darley, D. J., Albracht, S. P., Gerfen, G. J., Golding, B. T., and Buckel, W. (1998) Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium, Biochemistry 37, 4105-4113.
    • (1998) Biochemistry , vol.37 , pp. 4105-4113
    • Bothe, H.1    Darley, D.J.2    Albracht, S.P.3    Gerfen, G.J.4    Golding, B.T.5    Buckel, W.6
  • 8
    • 0029841914 scopus 로고    scopus 로고
    • Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucleotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction
    • Gerfen, G. J., Licht, S., Willems, J.-P., Hoffman, B. M., and Stubbe, J. (1996) Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucleotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction, J. Am. Chem. Soc. 118, 8192-8197.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8192-8197
    • Gerfen, G.J.1    Licht, S.2    Willems, J.-P.3    Hoffman, B.M.4    Stubbe, J.5
  • 10
    • 0028899970 scopus 로고
    • Evidence from EPR spectroscopy of the participation of radical intermediates in the reaction catalyzed by methylmalonyl-CoA mutase
    • Padmakumar, R., and Banerjee, R. (1995) Evidence from EPR spectroscopy of the participation of radical intermediates in the reaction catalyzed by methylmalonyl-CoA mutase, J. Biol. Chem. 270, 9295-9300.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9295-9300
    • Padmakumar, R.1    Banerjee, R.2
  • 11
    • 0030751379 scopus 로고    scopus 로고
    • Further insights into the mechanism of action of methylmalonyl-CoA mutase by electron paramagnetic resonance studies
    • Abend, A., Illich, V., and Retey, J. (1997) Further insights into the mechanism of action of methylmalonyl-CoA mutase by electron paramagnetic resonance studies, Eur. J. Biochem. 249, 180-186.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 180-186
    • Abend, A.1    Illich, V.2    Retey, J.3
  • 13
    • 0034614383 scopus 로고    scopus 로고
    • Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5,6-aminomutase from Clostridium sticklandii
    • Chang, C. H., and Frey, P. A. (2000) Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5,6-aminomutase from Clostridium sticklandii, J. Biol. Chem. 275, 106-114.
    • (2000) J. Biol. Chem. , vol.275 , pp. 106-114
    • Chang, C.H.1    Frey, P.A.2
  • 15
    • 0033566661 scopus 로고    scopus 로고
    • Glutamate mutase from Clostridium cochlearium: The structure of a coenzyme B12-dependent enzyme provides new mechanistic insights
    • Reitzer, R., Gruber, K., Jogl, G., Wagner, U. G., Bothe, H., Buckel, W., and Kratky, C. (1999) Glutamate mutase from Clostridium cochlearium: The structure of a coenzyme B12-dependent enzyme provides new mechanistic insights, Struct. Folding Des. 7, 891-902.
    • (1999) Struct. Folding Des. , vol.7 , pp. 891-902
    • Reitzer, R.1    Gruber, K.2    Jogl, G.3    Wagner, U.G.4    Bothe, H.5    Buckel, W.6    Kratky, C.7
  • 16
    • 0027485559 scopus 로고
    • A Rapid Method for the synthesis of methylmalonyl-Coenzyme a and other CoA-esters
    • Padmakumar, R., Gantla, S., and Banerjee, R. (1993) A Rapid Method for the synthesis of methylmalonyl-Coenzyme A and other CoA-esters, Anal. Biochem. 214, 318-320.
    • (1993) Anal. Biochem. , vol.214 , pp. 318-320
    • Padmakumar, R.1    Gantla, S.2    Banerjee, R.3
  • 17
    • 0034801511 scopus 로고    scopus 로고
    • Remarkably broad substrate tolerance of malonyl-CoA synthetase, an enzyme capable of intracellular synthesis of polyketide precursors
    • Pohl, N. L., Hans, M., Lee, H. Y., Kim, Y. S., Cane, D. E., and Khosla, C. (2001) Remarkably broad substrate tolerance of malonyl-CoA synthetase, an enzyme capable of intracellular synthesis of polyketide precursors, J. Am. Chem. Soc. 123, 5822-5823.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5822-5823
    • Pohl, N.L.1    Hans, M.2    Lee, H.Y.3    Kim, Y.S.4    Cane, D.E.5    Khosla, C.6
  • 18
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • Kauppinen, J. K., Moffatt, D. J., Manisch, H. H., and Cameron, D. G. (1981) Fourier self-deconvolution: A method for resolving intrinsically overlapped bands, Appl. Spectrosc. 35, 271-276.
    • (1981) Appl. Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Manisch, H.H.3    Cameron, D.G.4
  • 19
    • 0026650783 scopus 로고
    • Electron paramagnetic resonance studies of a ras p21-Mn(II)GDP complex in solution
    • Latwesen, D. G., Poe, M., Leigh, J. S., and Reed, G. H. (1992) Electron paramagnetic resonance studies of a ras p21-Mn(II)GDP complex in solution, Biochemistry 31, 4946-4950.
    • (1992) Biochemistry , vol.31 , pp. 4946-4950
    • Latwesen, D.G.1    Poe, M.2    Leigh, J.S.3    Reed, G.H.4
  • 21
    • 0033592455 scopus 로고    scopus 로고
    • Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: Mechanism-based inactivation by hydroxyethylhydrazine
    • Bandarian, V., and Reed, G. H. (1999) Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: Mechanism-based inactivation by hydroxyethylhydrazine, Biochemistry 38, 12394-12402.
    • (1999) Biochemistry , vol.38 , pp. 12394-12402
    • Bandarian, V.1    Reed, G.H.2
  • 23
    • 43949152886 scopus 로고
    • Global optimization of statistical functions with simulated annealing
    • Goffe, W. L., Ferrier, G. D., and Rogers, J. (1994) Global optimization of statistical functions with simulated annealing, J. Econometrics 60, 65-100.
    • (1994) J. Econometrics , vol.60 , pp. 65-100
    • Goffe, W.L.1    Ferrier, G.D.2    Rogers, J.3
  • 25
    • 0346850974 scopus 로고    scopus 로고
    • The positions of radical intermediates in the active sites of adenosylcobalamin-dependent enzymes
    • Reed, G. H., and Mansoorabadi, S. O. (2003) The positions of radical intermediates in the active sites of adenosylcobalamin-dependent enzymes, Curr. Opin. Struct. Biol. 13, 716-721.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 716-721
    • Reed, G.H.1    Mansoorabadi, S.O.2
  • 27
    • 33947484362 scopus 로고
    • Electron spin resonance spectra of oriented radicals
    • Morton, J. R. (1964) Electron spin resonance spectra of oriented radicals, Chem. Rev. 64, 453-471.
    • (1964) Chem. Rev. , vol.64 , pp. 453-471
    • Morton, J.R.1
  • 28
    • 0344095194 scopus 로고
    • 13C hyperfine interactions in radicals from some carboxylic acids
    • 13C hyperfine interactions in radicals from some carboxylic acids, J. Chem. Phys. 55, 5000-5008.
    • (1971) J. Chem. Phys. , vol.55 , pp. 5000-5008
    • Laroff, G.P.1    Fessenden, R.W.2
  • 29
    • 0000517176 scopus 로고
    • Kochi, J. K., Ed. John Wiley and Sons, New York
    • Fischer, H. (1973) in Free Radicals (Kochi, J. K., Ed.) pp 435-491, John Wiley and Sons, New York.
    • (1973) Free Radicals , pp. 435-491
    • Fischer, H.1
  • 31
    • 0032526407 scopus 로고    scopus 로고
    • Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism
    • Mancia, F., and Evans, P. (1998) Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism, Structure 6, 711-720.
    • (1998) Structure , vol.6 , pp. 711-720
    • Mancia, F.1    Evans, P.2
  • 32
    • 0026444094 scopus 로고
    • Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
    • Ballinger, M. D., Frey, P. A., and Reed, G. H. (1992) Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase, Biochemistry 31, 10782-10789.
    • (1992) Biochemistry , vol.31 , pp. 10782-10789
    • Ballinger, M.D.1    Frey, P.A.2    Reed, G.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.