메뉴 건너뛰기




Volumn 1707, Issue 1 SPEC. ISS., 2005, Pages 24-33

C-C bond formation and cleavage in radical enzymes, a theoretical perspective

Author keywords

Benzylsuccinate synthase; Density functional theory; Pyruvate formate lyase; Radical enzyme; Spore photoproduct lyase

Indexed keywords

BENZYLSUCCINATE SYNTHASE; ENZYME; FORMATE ACETYLTRANSFERASE; LYASE; RADICAL; SPORE PHOTOPRODUCT LYASE; UNCLASSIFIED DRUG;

EID: 13844280918     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.04.006     Document Type: Review
Times cited : (46)

References (28)
  • 1
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • Becke A.D. Density-functional exchange-energy approximation with correct asymptotic behavior. Phys. Rev. A38:1988;3098
    • (1988) Phys. Rev. , vol.38 , pp. 3098
    • Becke, A.D.1
  • 2
    • 77956779984 scopus 로고
    • Density-functional thermochemistry: 1. The effect of the exchange-only gradient correction
    • Becke A.D. Density-functional thermochemistry: 1. The effect of the exchange-only gradient correction. J. Chem. Phys. 96:1992;2155
    • (1992) J. Chem. Phys. , vol.96 , pp. 2155
    • Becke, A.D.1
  • 3
    • 0001161681 scopus 로고
    • Density-functional thermochemistry: 2. The effect of the Perdew-Wang generalized-gradient correlation correction
    • Becke A.D. Density-functional thermochemistry: 2. The effect of the Perdew-Wang generalized-gradient correlation correction. J. Chem. Phys. 97:1992;9173
    • (1992) J. Chem. Phys. , vol.97 , pp. 9173
    • Becke, A.D.1
  • 4
    • 0000189651 scopus 로고
    • Density-functional thermochemistry: 3. The role of exact exchange
    • Becke A.D. Density-functional thermochemistry: 3. The role of exact exchange. J. Chem. Phys. 98:1993;5648
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648
    • Becke, A.D.1
  • 6
    • 0038305457 scopus 로고    scopus 로고
    • Quantum chemical studies of radical-containing enzymes
    • Himo F., Siegbahn P.E.M. Quantum chemical studies of radical-containing enzymes. Chem. Rev. 103:2003;2421
    • (2003) Chem. Rev. , vol.103 , pp. 2421
    • Himo, F.1    Siegbahn, P.E.M.2
  • 7
    • 0001181339 scopus 로고    scopus 로고
    • Density functional theory of biologically relevant metal centers
    • Siegbahn P.E.M., Blomberg M.R.A. Density functional theory of biologically relevant metal centers. Annu. Rev. Phys. Chem. 50:1999;221
    • (1999) Annu. Rev. Phys. Chem. , vol.50 , pp. 221
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 8
    • 0035807631 scopus 로고    scopus 로고
    • A quantum chemical approach to the study of reaction mechanisms of redox-active metalloenzymes
    • Siegbahn P.E.M., Blomberg M.R.A. A quantum chemical approach to the study of reaction mechanisms of redox-active metalloenzymes. J. Phys. Chem., B. 105:2001;9375
    • (2001) J. Phys. Chem., B , vol.105 , pp. 9375
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 9
    • 0037295343 scopus 로고    scopus 로고
    • Mechanisms of metalloenzymes studied by quantum chemical methods
    • Siegbahn P.E.M. Mechanisms of metalloenzymes studied by quantum chemical methods. Q. Rev. Biophys. 36:2003;91
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 91
    • Siegbahn, P.E.M.1
  • 10
  • 15
    • 0037131403 scopus 로고    scopus 로고
    • X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA
    • Becker A., Kabsch W. X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. J. Biol. Chem. 277:2002;40036
    • (2002) J. Biol. Chem. , vol.277 , pp. 40036
    • Becker, A.1    Kabsch, W.2
  • 16
    • 0032508865 scopus 로고    scopus 로고
    • Catalytic mechanism of pyruvate formate-lyase; A theoretical study
    • Himo F., Eriksson L.A. Catalytic mechanism of pyruvate formate-lyase; a theoretical study. J. Am. Chem. Soc. 120:1998;11449
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11449
    • Himo, F.1    Eriksson, L.A.2
  • 17
    • 0001504129 scopus 로고    scopus 로고
    • Stability of protein-bound glycyl radical, a density functional theory study
    • Himo F. Stability of protein-bound glycyl radical, a density functional theory study. Chem. Phys. Lett. 328:2000;270
    • (2000) Chem. Phys. Lett. , vol.328 , pp. 270
    • Himo, F.1
  • 18
    • 0000887613 scopus 로고    scopus 로고
    • On the local geometry of glycyl radicals in different enzymes
    • Himo F., Eriksson L.A. On the local geometry of glycyl radicals in different enzymes. J. Chem. Soc., Perkin Trans. 2(2):1998;305
    • (1998) J. Chem. Soc., Perkin Trans. , vol.2 , Issue.2 , pp. 305
    • Himo, F.1    Eriksson, L.A.2
  • 19
    • 0024294291 scopus 로고
    • Inactivation of Escherichia coli pyruvate formate-lyase by hypophosphite: Evidence for a rate-limiting phosphorus-hydrogen bond cleavage
    • Brush E.J., Lipsett K.A., Kozarich J.W. Inactivation of Escherichia coli pyruvate formate-lyase by hypophosphite: evidence for a rate-limiting phosphorus-hydrogen bond cleavage. Biochemistry. 27:1988;2217
    • (1988) Biochemistry , vol.27 , pp. 2217
    • Brush, E.J.1    Lipsett, K.A.2    Kozarich, J.W.3
  • 22
    • 0033533642 scopus 로고    scopus 로고
    • Mechanistic studies on the repair of a novel DNA photolesion: The spore photoproduct
    • Mehl R.A., Begley T.P. Mechanistic studies on the repair of a novel DNA photolesion: the spore photoproduct. Org. Lett. 1:1999;1065
    • (1999) Org. Lett. , vol.1 , pp. 1065
    • Mehl, R.A.1    Begley, T.P.2
  • 23
    • 0035979231 scopus 로고    scopus 로고
    • The subunit structure and catalytic mechanism of the Bacillus subtilis DNA repair enzyme spore photoproduct lyase
    • Rebeil R., Nicholson W.L. The subunit structure and catalytic mechanism of the Bacillus subtilis DNA repair enzyme spore photoproduct lyase. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9038
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9038
    • Rebeil, R.1    Nicholson, W.L.2
  • 24
    • 0037181382 scopus 로고    scopus 로고
    • Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: Evidence for a reversibly generated adenosyl radical intermediate
    • Cheek J., Broderick J.B. Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: evidence for a reversibly generated adenosyl radical intermediate. J. Am. Chem. Soc. 124:2002;2860
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2860
    • Cheek, J.1    Broderick, J.B.2
  • 25
    • 0242355025 scopus 로고    scopus 로고
    • DNA repair by spore photoproduct lyase; A density functional theory study
    • Guo J.-D., Luo Y., Himo F. DNA repair by spore photoproduct lyase; a density functional theory study. J. Phys. Chem., B. 107:2003;11188
    • (2003) J. Phys. Chem., B. , vol.107 , pp. 11188
    • Guo, J.-D.1    Luo, Y.2    Himo, F.3
  • 26
    • 0031980567 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of benzylsuccinate synthase from thauera aromatica: A new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism
    • Leuthner B., Leutwein C., Schulz H., Hörth P., Haehnel W., Schilz E., Schägger H., Heider J. Biochemical and genetic characterization of benzylsuccinate synthase from thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol. Microbiol. 28:1998;615
    • (1998) Mol. Microbiol. , vol.28 , pp. 615
    • Leuthner, B.1    Leutwein, C.2    Schulz, H.3    Hörth, P.4    Haehnel, W.5    Schilz, E.6    Schägger, H.7    Heider, J.8
  • 27
    • 0035918166 scopus 로고    scopus 로고
    • A stable organic free radical in anaerobic benzylsuccinate synthase of Azoarcus sp. strain T
    • Krieger C.J., Roseboom W., Albracht S.P.J., Spormann A.M. A stable organic free radical in anaerobic benzylsuccinate synthase of Azoarcus sp. strain T. J. Biol. Chem. 276:2001;12924
    • (2001) J. Biol. Chem. , vol.276 , pp. 12924
    • Krieger, C.J.1    Roseboom, W.2    Albracht, S.P.J.3    Spormann, A.M.4
  • 28
    • 84961974056 scopus 로고    scopus 로고
    • Catalytic mechanism of benzylsuccinate synthase. A theoretical study
    • Himo F. Catalytic mechanism of benzylsuccinate synthase. A theoretical study. J. Phys. Chem., B. 106:2002;7688
    • (2002) J. Phys. Chem., B. , vol.106 , pp. 7688
    • Himo, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.