메뉴 건너뛰기




Volumn 22, Issue 5, 1998, Pages 523-541

Radical species in the catalytic pathways of enzymes from anaerobes

Author keywords

2 Hydroxyglutaryl CoA dehydratase; 4 Hydroxybutyryl CoA dehydratase; Benzoyl CoA reductase; Chorismate synthase; Coenzyme B12 dependent carbon skeleton mutase and eliminase; DNA photolyase; Lysine 2,3 aminomutase; Pyruvate formate lyase; Radical anion; Substrate based radical; Umpolung

Indexed keywords

DEOXYRIBODIPYRIMIDINE PHOTOLYASE; ENZYME; HYDROLYASE; LYASE; MUTASE; OXIDOREDUCTASE; RADICAL; SYNTHETASE;

EID: 0032466214     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(98)00038-2     Document Type: Review
Times cited : (55)

References (85)
  • 1
    • 0013593638 scopus 로고    scopus 로고
    • Hundert Jahre zellfreie Enzymologie, Eduard Buchner und die Zymase
    • [1] Jaenicke, L. (1997) Hundert Jahre zellfreie Enzymologie, Eduard Buchner und die Zymase. Biospektrum 3, 48-49.
    • (1997) Biospektrum , vol.3 , pp. 48-49
    • Jaenicke, L.1
  • 2
    • 0013565904 scopus 로고
    • Biosynthesis of fatty acids and cholesterol considered as chemical processes
    • [2] Cornforth, W. (1959) Biosynthesis of fatty acids and cholesterol considered as chemical processes. J. Lipid Res. 1, 3-28.
    • (1959) J. Lipid Res. , vol.1 , pp. 3-28
    • Cornforth, W.1
  • 3
    • 0000665162 scopus 로고
    • On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. V. Oxidations-reductions of the flavoproteins
    • [3] Beinert, H. and Page, E. (1957) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. V. Oxidations-reductions of the flavoproteins. J. Biol. Chem. 225, 479-497.
    • (1957) J. Biol. Chem. , vol.225 , pp. 479-497
    • Beinert, H.1    Page, E.2
  • 4
    • 0013619807 scopus 로고
    • Free radicals as intermediate steps of oxidation-reduction
    • [4] Michaelis, L. (1939) Free radicals as intermediate steps of oxidation-reduction. Cold Spring Harbor Symp. Quant. Biol. 7, 33-49.
    • (1939) Cold Spring Harbor Symp. Quant. Biol. , vol.7 , pp. 33-49
    • Michaelis, L.1
  • 6
    • 0032511425 scopus 로고    scopus 로고
    • 450-catalysed hydroxylation reactions. Implications for the cationic pathway
    • 450-catalysed hydroxylation reactions. Implications for the cationic pathway. J. Am. Chem. Soc. 120, 7719-7729.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7719-7729
    • Toy, P.H.1    Newcomb, M.2    Hollenberg, P.F.3
  • 7
    • 0032559208 scopus 로고    scopus 로고
    • Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl-radical reactivity
    • [7] Wang, Y., DuBois, J.L., Hedman, B., Hodgson, K.O. and Stack, T.D.P. (1998) Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl-radical reactivity. Science 279, 537-540.
    • (1998) Science , vol.279 , pp. 537-540
    • Wang, Y.1    DuBois, J.L.2    Hedman, B.3    Hodgson, K.O.4    Stack, T.D.P.5
  • 8
    • 0000817586 scopus 로고    scopus 로고
    • Warum besitzt die aktive Form der Galactose Oxidase einen diamagnetischen Grundzustand?
    • [8] Müller, J., Weyhermüller, Th., Bill, E., Hildebrandt, P., Ould-Moussa, L., Glaser, Th. and Wieghardt, K. (1998) Warum besitzt die aktive Form der Galactose Oxidase einen diamagnetischen Grundzustand? Angew. Chem. 110, 637-640; Angew. Chem. Int. Edn. Engl. 37, 616-619.
    • (1998) Angew. Chem. , vol.110 , pp. 637-640
    • Müller, J.1    Weyhermüller, T.2    Bill, E.3    Hildebrandt, P.4    Ould-Moussa, L.5    Glaser, T.6    Wieghardt, K.7
  • 9
    • 0013620869 scopus 로고    scopus 로고
    • [8] Müller, J., Weyhermüller, Th., Bill, E., Hildebrandt, P., Ould-Moussa, L., Glaser, Th. and Wieghardt, K. (1998) Warum besitzt die aktive Form der Galactose Oxidase einen diamagnetischen Grundzustand? Angew. Chem. 110, 637-640; Angew. Chem. Int. Edn. Engl. 37, 616-619.
    • Angew. Chem. Int. Edn. Engl. , vol.37 , pp. 616-619
  • 10
    • 0019162054 scopus 로고
    • A stable free radical intermediate in the reaction of 2-oxoacid:Ferredoxin oxidoreductases of Halobacterium halobium
    • [9] Cammack, R., Kerscher, L. and Oesterhelt, D. (1980) A stable free radical intermediate in the reaction of 2-oxoacid:ferredoxin oxidoreductases of Halobacterium halobium. FEBS Lett. 118, 271-273.
    • (1980) FEBS Lett. , vol.118 , pp. 271-273
    • Cammack, R.1    Kerscher, L.2    Oesterhelt, D.3
  • 11
    • 0030797482 scopus 로고    scopus 로고
    • Mechanism of the Clostridium thermoaceticum pyruvate:Ferredoxin oxidoreductase: Evidence for the common catalytic intermediacy of the hydroxyethylthiamine pyrophosphate radical
    • [10] Menon, S. and Ragsdale, S.W. (1997) Mechanism of the Clostridium thermoaceticum pyruvate:ferredoxin oxidoreductase: Evidence for the common catalytic intermediacy of the hydroxyethylthiamine pyrophosphate radical. Biochemistry 36, 8484-8494.
    • (1997) Biochemistry , vol.36 , pp. 8484-8494
    • Menon, S.1    Ragsdale, S.W.2
  • 12
    • 0030879399 scopus 로고    scopus 로고
    • Electron-nuclear double resonance spectroscopy investigation of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: Comparison with other flavin radical enzymes
    • [11] Çinkaya, I., Buckel, W., Medina, M.M., Gomez-Moreno, C. and Cammack, R. (1997) Electron-nuclear double resonance spectroscopy investigation of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: Comparison with other flavin radical enzymes. J. Biol. Chem. 378, 843-849.
    • (1997) J. Biol. Chem. , vol.378 , pp. 843-849
    • Çinkaya, I.1    Buckel, W.2    Medina, M.M.3    Gomez-Moreno, C.4    Cammack, R.5
  • 13
    • 0024601564 scopus 로고
    • Mechanism of flavoprotein-catalyzed reactions (Review)
    • [12] Ghisla, S. and Massey, V. (1989) Mechanism of flavoprotein-catalyzed reactions (Review). Eur. J. Biochem. 181, 1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 15
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • [14] Licht, S., Gerfen, G.J. and Stubbe, J. (1996) Thiyl radicals in ribonucleotide reductases. Science 271, 477-481.
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 16
    • 0026444094 scopus 로고
    • Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
    • [15] 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
  • 17
    • 0000944732 scopus 로고
    • Amino mutases
    • Dolphin, D., Ed., Wiley, New York, NY
    • 12, Vol. 2 (Dolphin, D., Ed.), pp. 203-232. Wiley, New York, NY.
    • (1982) 12 , vol.2 , pp. 203-232
    • Baker, J.J.1    Stadtman, T.C.2
  • 18
    • 0028172856 scopus 로고
    • 12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli
    • 12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Eur. J. Biochem. 266, 577-585.
    • (1994) Eur. J. Biochem. , vol.266 , pp. 577-585
    • Zelder, O.1    Beatrix, B.2    Leutbecher, U.3    Buckel, W.4
  • 20
    • 0015994398 scopus 로고
    • Two pathways of glutamate fermentation by anaerobic bacteria
    • [19] Buckel, W. and Barker, H.A. (1974) Two pathways of glutamate fermentation by anaerobic bacteria. J. Bacteriol. 117, 1248-1260.
    • (1974) J. Bacteriol. , vol.117 , pp. 1248-1260
    • Buckel, W.1    Barker, H.A.2
  • 21
    • 0014768391 scopus 로고
    • Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of α-methyleneglutaric acid to dimethylmaleic acid
    • [20] Kung, H.-F., Cederbaum, S., Tsai, L. and Stadtman, T.C. (1970) Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of α-methyleneglutaric acid to dimethylmaleic acid. Proc. Natl. Acad. Sci. USA 65, 978-984.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.65 , pp. 978-984
    • Kung, H.-F.1    Cederbaum, S.2    Tsai, L.3    Stadtman, T.C.4
  • 23
    • 0000549033 scopus 로고
    • Methylmalonyl-CoA mutase
    • Dolphin, D., Ed., Wiley, New York, NY
    • 12, Vol. 2 (Dolphin, D., Ed.), pp. 357-379, Wiley, New York, NY.
    • (1982) 12 , vol.2 , pp. 357-379
    • Retey, J.1
  • 25
    • 0032526407 scopus 로고    scopus 로고
    • Conformational changes on substrate binding to methylmalonyl-CoA mutase and new insights into free radical mechanism
    • [24] Mancia, F. and Evans, P.R. (1998) Conformational changes on substrate binding to methylmalonyl-CoA mutase and new insights into free radical mechanism. Structure 6, 711-720.
    • (1998) Structure , vol.6 , pp. 711-720
    • Mancia, F.1    Evans, P.R.2
  • 28
    • 0028794893 scopus 로고    scopus 로고
    • 12-dependent carbon skeleton rearrangements. Angew. Chem. 107, 2573-2576; Angew. Chem. Int. Edn. Engl. 34, 2398-2401.
    • Angew. Chem. Int. Edn. Engl. , vol.34 , pp. 2398-2401
  • 29
    • 0030751379 scopus 로고    scopus 로고
    • Further insights into the mechanism of action of methylmalonyl-CoA mutase by electron paramagnetic resonance studies
    • [27] Abend, A., Illich, V. and Rétey, 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    Rétey, J.3
  • 30
    • 0028097047 scopus 로고
    • Electron paramagnetic resonance studies of the methylmalonyl-CoA mutase reaction. Evidence for radical intermediates using natural and artificial substrates as well as the competitive inhibitor 3-carboxypropyl-CoA
    • [28] Zhao, Y., Abend, A., Kunz, M., Such, P. and Rétey, J. (1994) Electron paramagnetic resonance studies of the methylmalonyl-CoA mutase reaction. Evidence for radical intermediates using natural and artificial substrates as well as the competitive inhibitor 3-carboxypropyl-CoA. Eur. J. Biochem. 225, 891-896.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 891-896
    • Zhao, Y.1    Abend, A.2    Kunz, M.3    Such, P.4    Rétey, J.5
  • 31
    • 0028899970 scopus 로고
    • Evidence from electron paramagnetic resonance spectroscopy of the participation of radical intermediates in the reaction catalyzed by methylmalonyl-CoA mutase
    • [29] Padmakumar, R. and Banerjee, R. (1995) Evidence from electron paramagnetic resonance 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
  • 32
    • 0001479241 scopus 로고
    • Glutamate mutase
    • Dolphin, D., Ed., Wiley, New York, NY
    • 12 Vol. 2 (Dolphin, D., Ed.), pp. 289-355, Wiley, New York, NY.
    • (1982) 12 , vol.2 , pp. 289-355
    • Switzer, R.L.1
  • 35
    • 37049136984 scopus 로고
    • Radicals formed from acetylenes by high energy radiation and hydrogen atom bombardment: An electron spin resonance study
    • [33] Neilson, G.W. and Symons, M.C.R. (1973) Radicals formed from acetylenes by high energy radiation and hydrogen atom bombardment: an electron spin resonance study. J. Chem. Soc. Perkin Trans. 2, 1405-1410.
    • (1973) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1405-1410
    • Neilson, G.W.1    Symons, M.C.R.2
  • 36
    • 0032514774 scopus 로고    scopus 로고
    • Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase
    • [34] Thomä, N.H., Meier, T.W., Evans, P.R. and Leadlay, P.F. (1998) Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase. Biochemistry 37, 14386-14393.
    • (1998) Biochemistry , vol.37 , pp. 14386-14393
    • Thomä, N.H.1    Meier, T.W.2    Evans, P.R.3    Leadlay, P.F.4
  • 37
    • 0001210116 scopus 로고
    • The problem of rearrangement of β-alkyl radicals
    • [35] Bertini, F., Caronna, T., Grossi, L. and Minisci, F. (1974) The problem of rearrangement of β-alkyl radicals. Gazz. Chim. Ital. 104, 471-478.
    • (1974) Gazz. Chim. Ital. , vol.104 , pp. 471-478
    • Bertini, F.1    Caronna, T.2    Grossi, L.3    Minisci, F.4
  • 38
    • 33748599312 scopus 로고    scopus 로고
    • Radical-chain addition of aldehydes to alkenes catalysed by thiols
    • [36] Dang, H.-S. and Roberts, B.P. (1998) Radical-chain addition of aldehydes to alkenes catalysed by thiols. J. Chem. Soc. Perkin Trans. 1, 67-75.
    • (1998) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 67-75
    • Dang, H.-S.1    Roberts, B.P.2
  • 39
    • 0000565743 scopus 로고
    • CC bond formation reactions with umpolung of aldehydes via radicals
    • [37] Giese, B. and Horler, H. (1983) CC bond formation reactions with umpolung of aldehydes via radicals. Tetrahedron Lett. 24, 3221-3224.
    • (1983) Tetrahedron Lett. , vol.24 , pp. 3221-3224
    • Giese, B.1    Horler, H.2
  • 40
    • 0024278407 scopus 로고    scopus 로고
    • The error in the cryptic stereospecificity of methylmalonyl-CoA mutase. The use of carba-(dethia)-coenzyme A substrate analogues gives new insight into the enzyme mechanism
    • [38] Hull, W.E., Michenfelder, M. and Rétey, J. (1998) The error in the cryptic stereospecificity of methylmalonyl-CoA mutase. The use of carba-(dethia)-coenzyme A substrate analogues gives new insight into the enzyme mechanism. Eur. J. Biochem. 173, 191-210.
    • (1998) Eur. J. Biochem. , vol.173 , pp. 191-210
    • Hull, W.E.1    Michenfelder, M.2    Rétey, J.3
  • 41
    • 0013615006 scopus 로고    scopus 로고
    • 12: Theoretical studies of the 2-methyleneneglutarate-mutase-catalyzed rearrangement
    • in press
    • 12: Theoretical studies of the 2-methyleneneglutarate-mutase-catalyzed rearrangement. J. Am. Chem. Soc., in press.
    • (1998) J. Am. Chem. Soc.
    • Smith, D.M.1    Golding, B.T.2    Radom, L.3
  • 42
    • 0031980567 scopus 로고    scopus 로고
    • Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: A new glycyl-radical enzyme catalysing the first step in anaerobic toluene degradation
    • [40] Leuthner, B., Leutwein, C., Schulz, H., Hörth, P., Haehnel W., Schiltz, E., Schägger, H. and Heider, J. (1998) Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: a new glycyl-radical enzyme catalysing the first step in anaerobic toluene degradation. Mol. Microbiol. 28, 615-628.
    • (1998) Mol. Microbiol. , vol.28 , pp. 615-628
    • Leuthner, B.1    Leutwein, C.2    Schulz, H.3    Hörth, P.4    Haehnel, W.5    Schiltz, E.6    Schägger, H.7    Heider, J.8
  • 43
    • 0001346392 scopus 로고
    • One electron reactions of CoASH esters in anaerobic bacteria
    • [41] Buckel, W. and Keese, R. (1995) One electron reactions of CoASH esters in anaerobic bacteria. Angew. Chem. 107, 1595-1598; Angew. Chem. Int. Edn. Engl. 34, 1502-1506.
    • (1995) Angew. Chem. , vol.107 , pp. 1595-1598
    • Buckel, W.1    Keese, R.2
  • 44
    • 0003176221 scopus 로고    scopus 로고
    • [41] Buckel, W. and Keese, R. (1995) One electron reactions of CoASH esters in anaerobic bacteria. Angew. Chem. 107, 1595-1598; Angew. Chem. Int. Edn. Engl. 34, 1502-1506.
    • Angew. Chem. Int. Edn. Engl. , vol.34 , pp. 1502-1506
  • 45
    • 0030600142 scopus 로고    scopus 로고
    • Unusual dehydrations in anaerobic bacteria: Considering ketyls (radical anions) as reactive intermediates in enzymatic reactions
    • [42] Buckel, W. (1996) Unusual dehydrations in anaerobic bacteria: Considering ketyls (radical anions) as reactive intermediates in enzymatic reactions. FEBS Lett. 389, 20-24.
    • (1996) FEBS Lett. , vol.389 , pp. 20-24
    • Buckel, W.1
  • 46
    • 0001869573 scopus 로고    scopus 로고
    • Anaerobic energy metabolism
    • Chapter 12 (Lengeler, F., Drews, G. and Schlegel, H.G., Eds.), Thieme, Stuttgart, in press
    • [43] Buckel, W. (1999) Anaerobic energy metabolism. In: The Biology of Procaryotes, Chapter 12 (Lengeler, F., Drews, G. and Schlegel, H.G., Eds.), Thieme, Stuttgart, in press.
    • (1999) The Biology of Procaryotes
    • Buckel, W.1
  • 47
    • 0023515371 scopus 로고
    • Purification of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans: An iron sulfur protein
    • [44] Schweiger, G., Dutscho, R. and Buckel, W. (1987) Purification of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans: an iron sulfur protein. Eur. J. Biochem. 169, 441-448.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 441-448
    • Schweiger, G.1    Dutscho, R.2    Buckel, W.3
  • 48
    • 0001728892 scopus 로고
    • Methoden der Reaktivitätsumpolung
    • [45] Seebach, D. (1979) Methoden der Reaktivitätsumpolung. Angew. Chem. 91, 259-278; Angew. Chem. Int. Edn. Engl. 18, 239-258.
    • (1979) Angew. Chem. , vol.91 , pp. 259-278
    • Seebach, D.1
  • 49
    • 33746418283 scopus 로고    scopus 로고
    • [45] Seebach, D. (1979) Methoden der Reaktivitätsumpolung. Angew. Chem. 91, 259-278; Angew. Chem. Int. Edn. Engl. 18, 239-258.
    • Angew. Chem. Int. Edn. Engl. , vol.18 , pp. 239-258
  • 51
    • 0029040983 scopus 로고
    • Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • [47] Müller, U. and Buckel, W. (1995) Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Eur. J. Biochem. 230, 698-704.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 698-704
    • Müller, U.1    Buckel, W.2
  • 52
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • [48] Beinert, H., Holm, R.H. and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277, 653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 53
    • 0027934012 scopus 로고
    • Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: Correlation of the cluster type with enzymatic activity
    • [49] Hofmeister, A.E.M., Albracht, S.P.J. and Buckel, W. (1994) Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: correlation of the cluster type with enzymatic activity. FEBS Lett. 351, 416-418.
    • (1994) FEBS Lett. , vol.351 , pp. 416-418
    • Hofmeister, A.E.M.1    Albracht, S.P.J.2    Buckel, W.3
  • 54
    • 0027494834 scopus 로고
    • Nitrogenase metalloclusters: Structures, organization, and synthesis
    • [50] Dean, D.R., Bolin, J.T. and Zheng, L. (1993) Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 175, 6737-6744.
    • (1993) J. Bacteriol. , vol.175 , pp. 6737-6744
    • Dean, D.R.1    Bolin, J.T.2    Zheng, L.3
  • 55
    • 0016612419 scopus 로고
    • Substrate stereochemistry of the hydroxymethylglutaryl-CoA lyase and methylglutaconyl-CoA hydratase reactions
    • [51] Messner, B., Eggerer, H., Cornforth, J.W. and Mallaby, R. (1975) Substrate stereochemistry of the hydroxymethylglutaryl-CoA lyase and methylglutaconyl-CoA hydratase reactions. Eur. J. Biochem. 53, 255-264.
    • (1975) Eur. J. Biochem. , vol.53 , pp. 255-264
    • Messner, B.1    Eggerer, H.2    Cornforth, J.W.3    Mallaby, R.4
  • 56
    • 0016699732 scopus 로고
    • Substrate stereochemistry of the enoyl-CoA hydratase reaction
    • [52] Willadsen, P. and Eggerer, H. (1975) Substrate stereochemistry of the enoyl-CoA hydratase reaction. Eur. J. Biochem. 54, 247-252.
    • (1975) Eur. J. Biochem. , vol.54 , pp. 247-252
    • Willadsen, P.1    Eggerer, H.2
  • 57
    • 0025900515 scopus 로고
    • Crotonase-catalyzed β-elimination is concerted: A double isotope effect study
    • [53] Bahnson, B.J. and Anderson, V.E. (1991) Crotonase-catalyzed β-elimination is concerted: a double isotope effect study. Biochemistry 30, 5894-5906.
    • (1991) Biochemistry , vol.30 , pp. 5894-5906
    • Bahnson, B.J.1    Anderson, V.E.2
  • 58
    • 0029557669 scopus 로고
    • Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K 172
    • [54] Boll, M. and Fuchs, G. (1995) Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K 172. Eur. J. Biochem. 234, 921-933.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 921-933
    • Boll, M.1    Fuchs, G.2
  • 60
    • 0032528965 scopus 로고    scopus 로고
    • Genes coding for the benzoyl-CoA pathway of anaerobic metabolism in the bacterium Thauera aromatica
    • [56] Breese, K., Boll, M., Alt-Mörbe, J., Schägger, H. and Fuchs, G. (1998) Genes coding for the benzoyl-CoA pathway of anaerobic metabolism in the bacterium Thauera aromatica. Eur. J. Biochem. 256, 148-154.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 148-154
    • Breese, K.1    Boll, M.2    Alt-Mörbe, J.3    Schägger, H.4    Fuchs, G.5
  • 61
    • 85021603828 scopus 로고
    • Evidence from photoinduced EPR for a radical intermediate during photolysis of cyclobutane thymine dimer by DNA photolyase
    • [57] Kim, S.-T., Sancar, A., Essenmacher, C. and Babcock, G.T. (1992) Evidence from photoinduced EPR for a radical intermediate during photolysis of cyclobutane thymine dimer by DNA photolyase. J. Am. Chem. Soc. 114, 4442-4443.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4442-4443
    • Kim, S.-T.1    Sancar, A.2    Essenmacher, C.3    Babcock, G.T.4
  • 62
    • 0029967883 scopus 로고    scopus 로고
    • Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase
    • [58] Macheroux, P., Bornemann, S., Ghisla, S. and Thorneley, R.N. (1996) Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase. J. Biol. Chem. 271, 25850-25858.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25850-25858
    • Macheroux, P.1    Bornemann, S.2    Ghisla, S.3    Thorneley, R.N.4
  • 63
    • 0028204034 scopus 로고
    • A model for the chorismate synthase
    • [59] Giese, B. and Almstead, N.G. (1994) A model for the chorismate synthase. Tetrahedron Lett. 35, 1677-1680.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 1677-1680
    • Giese, B.1    Almstead, N.G.2
  • 64
    • 0027272487 scopus 로고
    • Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ2-Δ3-isomerase from Clostridium aminobutyricum
    • [60] Scherf, U. and Buckel, W. (1993) Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ2-Δ3-isomerase from Clostridium aminobutyricum. Eur. J. Biochem. 215, 421-429.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 421-429
    • Scherf, U.1    Buckel, W.2
  • 65
    • 0029828449 scopus 로고    scopus 로고
    • 4-Hydroxybutyryl-CoA-dehydratase from Clostridium aminobutyricum: The roles of FAD and iron-sulfur clusters in an overall non-redox reaction
    • [61] Müh, U., Cinkaya, I., Albracht, S.P.J. and Buckel, W. (1996) 4-Hydroxybutyryl-CoA-dehydratase from Clostridium aminobutyricum: the roles of FAD and iron-sulfur clusters in an overall non-redox reaction. Biochemistry 35, 11710-11718.
    • (1996) Biochemistry , vol.35 , pp. 11710-11718
    • Müh, U.1    Cinkaya, I.2    Albracht, S.P.J.3    Buckel, W.4
  • 66
    • 0030613554 scopus 로고    scopus 로고
    • Mössbauer study of 4-hydroxybutyryl-CoA dehydratase: Probing the role of an iron-sulfur cluster in an overall non-redox reaction
    • [62] Müh, U., Bill, E. and Buckel, W. (1997) Mössbauer study of 4-hydroxybutyryl-CoA dehydratase: probing the role of an iron-sulfur cluster in an overall non-redox reaction. Eur. J. Biochem. 248, 380-384.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 380-384
    • Müh, U.1    Bill, E.2    Buckel, W.3
  • 67
  • 68
    • 0000671274 scopus 로고
    • Double isotope fractionation: Test for concertedness and for transition-state dominance
    • [64] Belasco, J.G., Albery, W.J. and Knowles, J.R. (1983) Double isotope fractionation: test for concertedness and for transition-state dominance. J. Am. Chem. Soc. 105, 2475-2477.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2475-2477
    • Belasco, J.G.1    Albery, W.J.2    Knowles, J.R.3
  • 69
    • 0020492976 scopus 로고
    • Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase
    • [65] Hermes, J.D., Roeske, C.A., O'Leary, M.H. and Cleland, W.W. (1982) Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase. Biochemistry 21, 5106-5114.
    • (1982) Biochemistry , vol.21 , pp. 5106-5114
    • Hermes, J.D.1    Roeske, C.A.2    O'Leary, M.H.3    Cleland, W.W.4
  • 70
    • 0025900515 scopus 로고
    • Crotonase-catalyzed β-elimination is concerted: A double isotope effect study
    • [66] Bahnson, B.J. and Anderson, V.E. (1991) Crotonase-catalyzed β-elimination is concerted: a double isotope effect study. Biochemistry 30, 5894-5906.
    • (1991) Biochemistry , vol.30 , pp. 5894-5906
    • Bahnson, B.J.1    Anderson, V.E.2
  • 71
    • 77954165734 scopus 로고
    • Formation and stability of reactive intermediates of organic reactions in aqueous solution
    • Golding, B.T., Griffin, R.J. and Maskill, H., Eds., Royal Society of Chemistry, Cambridge
    • [67] Amyes, T.L., Richard, J.P. and Jagannadham, V. (1995) Formation and stability of reactive intermediates of organic reactions in aqueous solution. In: Organic Reactivity: Physical and Biological Aspects (Golding, B.T., Griffin, R.J. and Maskill, H., Eds.), pp. 334-350. Royal Society of Chemistry, Cambridge.
    • (1995) Organic Reactivity: Physical and Biological Aspects , pp. 334-350
    • Amyes, T.L.1    Richard, J.P.2    Jagannadham, V.3
  • 72
    • 0029076271 scopus 로고
    • Importance of historical contingency in the stereochemistry of hydratase-dehydratase enzymes
    • [68] Mohrig, J.R., Moerke, K.A., Cloutier, D.L., Lane, B.D., Person, E.C. and Onasch, T.B. (1995) Importance of historical contingency in the stereochemistry of hydratase-dehydratase enzymes. Science 269, 527-529.
    • (1995) Science , vol.269 , pp. 527-529
    • Mohrig, J.R.1    Moerke, K.A.2    Cloutier, D.L.3    Lane, B.D.4    Person, E.C.5    Onasch, T.B.6
  • 74
    • 0022401026 scopus 로고
    • p-Cresol formation by cell-free extracts of Clostridium difficile
    • [70] D'Ari, L. and Barker, H.A. (1985) p-Cresol formation by cell-free extracts of Clostridium difficile. Arch. Microbiol. 143, 311-312.
    • (1985) Arch. Microbiol. , vol.143 , pp. 311-312
    • D'Ari, L.1    Barker, H.A.2
  • 75
    • 0031988007 scopus 로고    scopus 로고
    • Toxins from anaerobic bacteria: Specificity and molecular mechanisms of action
    • [71] Boquet, P., Munro, P., Fiorentini, C. and Just, I. (1998) Toxins from anaerobic bacteria: specificity and molecular mechanisms of action. Curr. Opin. Microbiol. 1, 66-74.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 66-74
    • Boquet, P.1    Munro, P.2    Fiorentini, C.3    Just, I.4
  • 76
    • 0000830511 scopus 로고
    • Post-translational activation introduces a free radical into pyruvate formate-lyase
    • [72] Knappe, J., Neugebauer, F.A., Blaschkowski, H.P. and Gänzler, M. (1984) Post-translational activation introduces a free radical into pyruvate formate-lyase. Proc. Natl. Acad. Sci. USA 81, 1332-1335.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1332-1335
    • Knappe, J.1    Neugebauer, F.A.2    Blaschkowski, H.P.3    Gänzler, M.4
  • 77
    • 0013566306 scopus 로고    scopus 로고
    • This volume
    • [73] Sawers, G. (1998) This volume.
    • (1998)
    • Sawers, G.1
  • 78
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • [74] Stubbe, J. and van der Donk, W.A. (1998) Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762.
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 79
    • 0000198545 scopus 로고
    • 12 coenzyme: Theory and models
    • Dolphin, D., Ed., Wiley, New York, NY
    • 12, Vol. 1 (Dolphin, D., Ed.), pp. 543-582. Wiley, New York, NY.
    • (1982) 12 , vol.1 , pp. 543-582
    • Golding, B.T.1
  • 80
    • 0019182317 scopus 로고
    • On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli
    • [76] Stubbe, J. and Ackles, D. (1980) On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. J. Biol. Chem. 255, 8027-8030.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8027-8030
    • Stubbe, J.1    Ackles, D.2
  • 81
    • 0030891240 scopus 로고    scopus 로고
    • Studies on the mechanism of ribonucleotide reductases
    • [77] Lenz, R. and Giese, B. (1997) Studies on the mechanism of ribonucleotide reductases. J. Am. Chem. Soc. 119, 2784-2794.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2784-2794
    • Lenz, R.1    Giese, B.2
  • 82
    • 0001665934 scopus 로고
    • Enzymic reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates?
    • [78] Rétey, J. (1990) Enzymic reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates? Angew. Chem. 102, 373-379; Angew. Chem. Int. Edn. Engl. 29, 355-361.
    • (1990) Angew. Chem. , vol.102 , pp. 373-379
    • Rétey, J.1
  • 83
    • 0013591145 scopus 로고    scopus 로고
    • [78] Rétey, J. (1990) Enzymic reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates? Angew. Chem. 102, 373-379; Angew. Chem. Int. Edn. Engl. 29, 355-361.
    • Angew. Chem. Int. Edn. Engl. , vol.29 , pp. 355-361
  • 84
    • 0022350370 scopus 로고
    • Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase
    • [79] Kuchta, R.D. and Abeles, R.H. (1985) Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase. J. Biol. Chem. 260, 13181-13189.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13181-13189
    • Kuchta, R.D.1    Abeles, R.H.2
  • 85
    • 0026550360 scopus 로고
    • (R)-Lactyl-CoA dehydratase from Clostridium propionicum: Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA
    • [80] Hofmeister, A.E.M. and Buckel, W. (1992) (R)-Lactyl-CoA dehydratase from Clostridium propionicum: stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA. Eur. J. Biochem. 206, 547-552.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 547-552
    • Hofmeister, A.E.M.1    Buckel, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.