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Volumn 46, Issue 24, 2007, Pages 7293-7301

Dioldehydrase: An essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLCOBALAMIN; DIOLDEHYDRASE; HOMOLYTIC CLEAVAGE; MASS SPECTRAL ANALYSIS; NUCLEOSIDE;

EID: 34250857476     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700078z     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 73649177916 scopus 로고
    • Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme
    • Lee, H. A., and Abeles, R. H. (1963) Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme, J. Biol. Chem. 238, 2367-2373.
    • (1963) J. Biol. Chem , vol.238 , pp. 2367-2373
    • Lee, H.A.1    Abeles, R.H.2
  • 3
    • 0030668674 scopus 로고    scopus 로고
    • Propanediol utilization genes (pdu) of Salmonella typhimurium: Three genes for the propanediol dehydratase
    • Bobik, T. A., Xu, Y., Jeter, R. M., Otto, K. E., and Roth, J. R. (1997) Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes for the propanediol dehydratase, J. Bacteriol. 179, 6633-6639.
    • (1997) J. Bacteriol , vol.179 , pp. 6633-6639
    • Bobik, T.A.1    Xu, Y.2    Jeter, R.M.3    Otto, K.E.4    Roth, J.R.5
  • 6
    • 33747193400 scopus 로고
    • Thermolysis of adenosylcobalamin: A product, kinetic, and cobalt-carbon (C5′) bond dissociation energy study
    • Finke, R. G., and Hay, B. P. (1984) Thermolysis of adenosylcobalamin: a product, kinetic, and cobalt-carbon (C5′) bond dissociation energy study, Inorg. Chem. 23, 3041-3043.
    • (1984) Inorg. Chem , vol.23 , pp. 3041-3043
    • Finke, R.G.1    Hay, B.P.2
  • 7
    • 33845373586 scopus 로고
    • Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociation energy in aqueous solution
    • Hay, B. P., and Finke, R. G. (1986) Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociation energy in aqueous solution, J. Am. Chem. Soc 108, 4820-4829.
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 4820-4829
    • Hay, B.P.1    Finke, R.G.2
  • 8
    • 2742589922 scopus 로고
    • Thermolysis of the cobalt-carbon bond in adenosylcorrins. 3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis
    • Hay, B. P., and Finke, R. G. (1987) Thermolysis of the cobalt-carbon bond in adenosylcorrins. 3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis, J. Am. Chem. Soc. 109, 8012-8018.
    • (1987) J. Am. Chem. Soc , vol.109 , pp. 8012-8018
    • Hay, B.P.1    Finke, R.G.2
  • 9
    • 0000706235 scopus 로고
    • 12) - IV. Products, kinetics and Co-C bond dissociation energy studies in ethylene glycol
    • 12) - IV. Products, kinetics and Co-C bond dissociation energy studies in ethylene glycol, Polyhedron 7, 1469-1481.
    • (1988) Polyhedron , vol.7 , pp. 1469-1481
    • Hay, B.P.1    Finke, R.G.2
  • 10
    • 0001153340 scopus 로고
    • 12-dependent enzymes function as "ultimate radical cages" and "ultimate radical traps
    • 12-dependent enzymes function as "ultimate radical cages" and "ultimate radical traps", Inorg. Chem. 32, 4414-4421.
    • (1993) Inorg. Chem. 32 , pp. 4414-4421
    • Garr, C.D.1    Finke, R.G.2
  • 12
    • 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
  • 13
    • 0032566325 scopus 로고    scopus 로고
    • Coupling of cobalt-carbon bond homolysis and hydrogen atom abstraction in adenosylcobalamin-dependent glutamate mutase
    • 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.
    • (1998) Biochemistry , vol.37 , pp. 11864-11872
    • Marsh, E.N.G.1    Ballou, D.P.2
  • 14
    • 0014027350 scopus 로고
    • Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex
    • Wagner, O. W., Lee, H. A., Jr., Frey, P. A., and Abeles, R. H. (1966) Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex, J. Biol. Chem. 24, 1751-1762.
    • (1966) J. Biol. Chem , vol.24 , pp. 1751-1762
    • Wagner, O.W.1    Lee Jr., H.A.2    Frey, P.A.3    Abeles, R.H.4
  • 16
    • 34250827069 scopus 로고    scopus 로고
    • 5′-Peroxyadenosine and 5′-peroxyadenosylcobalamin as intermediates in the aerobic photolysis of adenosylcobalamin
    • Schwartz, P. A., and Frey, P. A. (2007) 5′-Peroxyadenosine and 5′-peroxyadenosylcobalamin as intermediates in the aerobic photolysis of adenosylcobalamin, Biochemistry 46, 7284-7292.
    • (2007) Biochemistry , vol.46 , pp. 7284-7292
    • Schwartz, P.A.1    Frey, P.A.2
  • 17
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and Richardson, C. C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes, Proc. Natl. Acad. Sci. U.S.A. 82, 1074-1078.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 18
    • 34249783479 scopus 로고    scopus 로고
    • Probing interactions from a solvent-exchangeable proton and monocations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase
    • submitted for publication
    • Schwartz, P. A., LoBrutto, R., Reed, G. H., and Frey, P. A. (2007) Probing interactions from a solvent-exchangeable proton and monocations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase, Protein Sci., submitted for publication.
    • (2007) Protein Sci
    • Schwartz, P.A.1    LoBrutto, R.2    Reed, G.H.3    Frey, P.A.4
  • 19
    • 0037022197 scopus 로고    scopus 로고
    • Interactions of diol dehydrase and 3′,4′-anhydroadenosylcobalamin: Suicide inactivation by electron transfer
    • Magnusson, O. T., and Frey, P. A. (2002) Interactions of diol dehydrase and 3′,4′-anhydroadenosylcobalamin: suicide inactivation by electron transfer, Biochemistry 41, 1695-1702.
    • (2002) Biochemistry , vol.41 , pp. 1695-1702
    • Magnusson, O.T.1    Frey, P.A.2
  • 20
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang, Z. -Y., Woollard, A. C. S., and Wolff, S. P. (1990) Hydrogen peroxide production during experimental protein glycation, FEBS Lett. 268, 69-71.
    • (1990) FEBS Lett , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 22
    • 0033576307 scopus 로고    scopus 로고
    • 12-dependent methylmalonyl-CoA mutase
    • 12-dependent methylmalonyl-CoA mutase, Biochemistry 38, 15287-15294.
    • (1999) Biochemistry , vol.38 , pp. 15287-15294
    • Chowdhury, S.1    Banerjee, R.2
  • 23
    • 0014764830 scopus 로고
    • Escherichia coli B 5-methyltetrahydrofolate- homocysteine cobalamin methyltransferase: Resolution and reconstitution of holoenzyme
    • Taylor, R. T. (1970) Escherichia coli B 5-methyltetrahydrofolate- homocysteine cobalamin methyltransferase: resolution and reconstitution of holoenzyme, Arch. Biochem. Biophys. 137, 529-546.
    • (1970) Arch. Biochem. Biophys , vol.137 , pp. 529-546
    • Taylor, R.T.1
  • 24
    • 0014429342 scopus 로고
    • Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. II. Physical and chemical properties and interaction with cobamides and ethanolamine
    • Kaplan, B. H., and Stadtman, E. R. (1968) Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. II. Physical and chemical properties and interaction with cobamides and ethanolamine, J. Biol. Chem. 243, 1794-1803.
    • (1968) J. Biol. Chem , vol.243 , pp. 1794-1803
    • Kaplan, B.H.1    Stadtman, E.R.2
  • 27
    • 0015504278 scopus 로고
    • 12-dependent propanediol dehydratase system ternary complex between apoenzyme, coenzyme, and substrate analog
    • 12-dependent propanediol dehydratase system ternary complex between apoenzyme, coenzyme, and substrate analog, Biochim. Biophys. Acta 284, 536-548.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 536-548
    • Toraya, T.1    Fukui, S.2
  • 29
    • 0028295773 scopus 로고    scopus 로고
    • 12 ethanolamine ammonia lyase: evidence for a radical mechanism, Science 263, 958-960.
    • 12 ethanolamine ammonia lyase: evidence for a radical mechanism, Science 263, 958-960.
  • 32
    • 0037461322 scopus 로고    scopus 로고
    • 2H]adenosylcobalamin by ribonucleoside triphosphate reductase: Cysteine 408-independent cleavage of the Co-C5′ bond
    • 2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5′ bond, Biochemistry 42, 4578-4584.
    • (2003) Biochemistry , vol.42 , pp. 4578-4584
    • Chen, D.1    Abend, A.2    Stubbe, J.3    Frey, P.A.4
  • 34
    • 84855620601 scopus 로고
    • Dolphin, D, Ed, Vols, and 2, Wiley-Interscience, New York
    • 12, Vols. 1 and 2, Wiley-Interscience, New York.
    • (1982) 12 , vol.1
  • 35
    • 0029959147 scopus 로고    scopus 로고
    • 12 via cobalt-carbon bond thermolysis product and kinetic studies as a function of exogenous pyridine bases
    • 12 via cobalt-carbon bond thermolysis product and kinetic studies as a function of exogenous pyridine bases, J. Am. Chem. Soc. 118, 11142-11154.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11142-11154
    • Garr, C.D.1    Sirovatka, J.M.2    Finke, R.G.3
  • 37
    • 0035340231 scopus 로고    scopus 로고
    • Electron transfer in the substrate-dependent suicide inactivation of lysine 5,6-aminomutase
    • Tang, K. H., Chang, C. H., and Frey, P. A. (2001) Electron transfer in the substrate-dependent suicide inactivation of lysine 5,6-aminomutase, Biochemistry 40, 5190-5199.
    • (2001) Biochemistry , vol.40 , pp. 5190-5199
    • Tang, K.H.1    Chang, C.H.2    Frey, P.A.3
  • 38
    • 0037022798 scopus 로고    scopus 로고
    • A novel reaction between adenosylcobalamin and 2-methylene-glutarate catalyzed by glutamate mutase
    • Huhta, M. S., Ciceri, D., Golding, B. T., and Marsh, E. N. (2002) A novel reaction between adenosylcobalamin and 2-methylene-glutarate catalyzed by glutamate mutase, Biochemistry 41, 3200-3206.
    • (2002) Biochemistry , vol.41 , pp. 3200-3206
    • Huhta, M.S.1    Ciceri, D.2    Golding, B.T.3    Marsh, E.N.4
  • 39
    • 3142546271 scopus 로고    scopus 로고
    • When a spectator turns killer: Suicidal electron transfer from cobalamin in methylmalonyl-CoA mutase
    • Vlasie, M. D., and Banerjee, R. (2004) When a spectator turns killer: suicidal electron transfer from cobalamin in methylmalonyl-CoA mutase, Biochemistry 43, 8410-8417.
    • (2004) Biochemistry , vol.43 , pp. 8410-8417
    • Vlasie, M.D.1    Banerjee, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.