메뉴 건너뛰기




Volumn , Issue , 2014, Pages 211-238

The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84927166656     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1515/9783110308426.211     Document Type: Chapter
Times cited : (7)

References (143)
  • 1
    • 0038360241 scopus 로고
    • Pyruvic acid metabolism. A factorrequired for oxidation by Streptococcus faecalis
    • O'Kane DJ, Gunsalus IC. Pyruvic acid metabolism. A factor required for oxidation by Streptococcus faecalis. J Bacteriol 1948;56:499-506.
    • (1948) J Bacteriol , vol.56 , pp. 499-506
    • O'Kane, D.J.1    Gunsalus, I.C.2
  • 2
    • 12544254294 scopus 로고
    • Pyruvic acid metabolism. III. A manometric assay for pyruvate oxidation factor
    • Gunsalus IC, Dolin MI, Struglia L. Pyruvic acid metabolism. III. A manometric assay for pyruvate oxidation factor. J Biol Chem 1952;194:849-57.
    • (1952) J Biol Chem , vol.194 , pp. 849-857
    • Gunsalus, I.C.1    Dolin, M.I.2    Struglia, L.3
  • 3
    • 0009471246 scopus 로고
    • The nutritional role of acetate for lactic acid bacteria. I. The response to substances related to acetate
    • Guirard BM, Snell EE, Williams RJ. The nutritional role of acetate for lactic acid bacteria. I. The response to substances related to acetate. Arch Biochem 1946;9:361-79.
    • (1946) Arch Biochem , vol.9 , pp. 361-379
    • Guirard, B.M.1    Snell, E.E.2    Williams, R.J.3
  • 4
    • 0000024075 scopus 로고
    • Discovery of a new acetate-replacing factor
    • Skeggs HR, Wright LD, Cresson EL, et al. Discovery of a new acetate-replacing factor. J Bacteriol 1956;72:519-24.
    • (1956) J Bacteriol , vol.72 , pp. 519-524
    • Skeggs, H.R.1    Wright, L.D.2    Cresson, E.L.3
  • 5
    • 0002908647 scopus 로고
    • Crystalline a-lipoic acid: A catalytic agent associated with pyruvate dehydrogenase
    • Reed LJ, Busk BGD, Gunsalus IC, Schnakenberg GHF. Crystalline a-lipoic acid: a catalytic agent associated with pyruvate dehydrogenase. Science 1951;114:93.
    • (1951) Science , vol.114 , pp. 93
    • Reed, L.J.1    Busk, B.2    Gunsalus, I.C.3    Schnakenberg, G.H.F.4
  • 6
    • 33947454425 scopus 로고
    • Isolation, characterization and structure of a-lipoic acid
    • Reed LJ, Gunsalus IC, Schnakenberg GHF, et al. Isolation, characterization and structure of a-lipoic acid. J Am Chem Soc 1953;75:1267-70.
    • (1953) J am Chem Soc , vol.75 , pp. 1267-1270
    • Reed, L.J.1    Gunsalus, I.C.2    Schnakenberg, G.3
  • 11
    • 0342999282 scopus 로고
    • The stereochemistry of a-lipoic acid
    • Mislow K, Meluch WC. The stereochemistry of a-lipoic acid. J Am Chem Soc 1956;78:5920.
    • (1956) J am Chem Soc , vol.78 , pp. 5920
    • Mislow, K.1    Meluch, W.C.2
  • 12
    • 0027934852 scopus 로고
    • Lipoic acid favors thiolsulfinate formation after hypochlorous acid scavenging: A study with lipoic acid derivatives
    • Biewenga GP, Dejong J, Bast A. Lipoic acid favors thiolsulfinate formation after hypochlorous acid scavenging: a study with lipoic acid derivatives. Arch Biochem Biophys 1994;312:114-20.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 114-120
    • Biewenga, G.P.1    Dejong, J.2    Bast, A.3
  • 13
    • 0016800742 scopus 로고
    • Lipoic acid content of Escherichia coli and other microorganisms
    • Herbert AA, Guest JR. Lipoic acid content of Escherichia coli and other microorganisms. Arch Biochem Biophys 1975;106:259-66.
    • (1975) Arch Biochem Biophys , vol.106 , pp. 259-266
    • Herbert, A.A.1    Guest, J.R.2
  • 14
    • 2642644904 scopus 로고
    • Multienzyme complexes
    • Reed LJ. Multienzyme complexes. Acc Chem Res 1974;7:40-6.
    • (1974) Acc Chem Res , vol.7 , pp. 40-46
    • Reed, L.J.1
  • 15
    • 0015893632 scopus 로고
    • Glycine metabolism. Lipoic acid as the prosthetic group in the electron transfer protein P2 from Peptococcus glycinophilus
    • Robinson JR, Klein SM, Sagers RD. Glycine metabolism. Lipoic acid as the prosthetic group in the electron transfer protein P2 from Peptococcus glycinophilus. J Biol Chem 1973;248:5319-23.
    • (1973) J Biol Chem , vol.248 , pp. 5319-5323
    • Robinson, J.R.1    Klein, S.M.2    Sagers, R.D.3
  • 16
    • 0007623841 scopus 로고
    • A-Keto acid dehydrogenation complexes. II. Therole of protein-bound lipoic acid and flavin adenine dinucleotide
    • Koike M, Reed LJ. a-Keto acid dehydrogenation complexes. II. The role of protein-bound lipoic acid and flavin adenine dinucleotide. J Biol Chem 1960;235:1931-8.
    • (1960) J Biol Chem , vol.235 , pp. 1931-1938
    • Koike, M.1    Reed, L.J.2
  • 17
    • 0001752523 scopus 로고
    • Studies on the nature and reactions of protein-bound lipoic acid
    • Reed LJ, Koike M, Levitch ME, Leach FR. Studies on the nature and reactions of protein-bound lipoic acid. J Biol Chem 1958;232:143-58.
    • (1958) J Biol Chem , vol.232 , pp. 143-158
    • Reed, L.J.1    Koike, M.2    Levitch, M.E.3    Leach, F.R.4
  • 18
    • 0019013615 scopus 로고
    • Kinetic analysis of the role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Ambrose-Griffen MC, Danson MJ, Griffen WG, Hale G, Perham RN. Kinetic analysis of the role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Biochem J 1980;187:393-401.
    • (1980) Biochem J , vol.187 , pp. 393-401
    • Ambrose-Griffen, M.C.1    Danson, M.J.2    Griffen, W.G.3    Hale, G.4    Perham, R.N.5
  • 19
    • 0018183337 scopus 로고
    • Mechanism of action of the pyruvate dehydrogenase multienzyme complex from Escherichia coli
    • Angelides KJ, Hammes GG. Mechanism of action of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Proc Natl Acad Sci USA 1978;75:4877-80.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4877-4880
    • Angelides, K.J.1    Hammes, G.G.2
  • 20
    • 2442728373 scopus 로고
    • Purification and characterization of branched chain a-keto acid dehydrogenase complex of bovine kidney
    • Pettit FH, Yeaman SJ, Reed LJ. Purification and characterization of branched chain a-keto acid dehydrogenase complex of bovine kidney. Proc Natl Acad Sci USA 1978;75:4881-5.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4881-4885
    • Pettit, F.H.1    Yeaman, S.J.2    Reed, L.J.3
  • 21
    • 0028341619 scopus 로고
    • Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system
    • Kruger N, Oppermann FB, Lorenzl H, Steinbuchel A. Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. J Bacteriol 1994;176:3614-30.
    • (1994) J Bacteriol , vol.176 , pp. 3614-3630
    • Kruger, N.1    Oppermann, F.B.2    Lorenzl, H.3    Steinbuchel, A.4
  • 22
    • 0025913664 scopus 로고
    • Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism
    • Priefert H, Hein S, Kruger N, Zeh K, Schmidt B, Steinbuchel A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J Bacteriol 1991;173:4056-71.
    • (1991) J Bacteriol , vol.173 , pp. 4056-4071
    • Priefert, H.1    Hein, S.2    Kruger, N.3    Zeh, K.4    Schmidt, B.5    Steinbuchel, A.6
  • 23
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perham RN. Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 1991;30:8501-12.
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 25
    • 0024459807 scopus 로고
    • Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney: Radial distribution of mass determined from dark-field electron micrographs
    • Hackert ML, Xu WX, Oliver RM, et al. Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney: radial distribution of mass determined from dark-field electron micrographs. Biochemistry 1989;28:6816-21.
    • (1989) Biochemistry , vol.28 , pp. 6816-6821
    • Hackert, M.L.1    Xu, W.X.2    Oliver, R.M.3
  • 26
    • 0040415533 scopus 로고
    • Intermediary metabolism of Diplococcus glycinophilus. I. Glycine cleavage and one-carbon interconversions
    • Sagers RD, Gunsalus IC. Intermediary metabolism of Diplococcus glycinophilus. I. Glycine cleavage and one-carbon interconversions. J Bacteriol 1961;81:541-9.
    • (1961) J Bacteriol , vol.81 , pp. 541-549
    • Sagers, R.D.1    Gunsalus, I.C.2
  • 27
    • 0021225114 scopus 로고
    • Mechanism of the glycine cleavage reaction. Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein
    • Fujiwara K, Okamura-Ikeda K, Motokawa Y. Mechanism of the glycine cleavage reaction. Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein. J Biol Chem 1984;259:10664-8.
    • (1984) J Biol Chem , vol.259 , pp. 10664-10668
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 28
    • 0019333268 scopus 로고
    • The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria
    • Hiraga K, Kikuchi G. The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria. J Biol Chem 1980;255:11664-70.
    • (1980) J Biol Chem , vol.255 , pp. 11664-11670
    • Hiraga, K.1    Kikuchi, G.2
  • 29
    • 0014216005 scopus 로고
    • Glycine metabolism. IV. Effect of borohydrine reduction on the pyridoxal phosphate-containing glycine decarboxylase from Peptococcus glycinophilus
    • Klein SM, Sagers RD. Glycine metabolism. IV. Effect of borohydrine reduction on the pyridoxal phosphate-containing glycine decarboxylase from Peptococcus glycinophilus. J Biol Chem 1967;242:301-5.
    • (1967) J Biol Chem , vol.242 , pp. 301-305
    • Klein, S.M.1    Sagers, R.D.2
  • 30
    • 0018792473 scopus 로고
    • Hydrogen carrier protein from chicken liver: Purification, characterization, and role of its prosthetic group, lipoic acid, in the glycine cleavage reaction
    • Fujiwara K, Okamura K, Motokawa Y. Hydrogen carrier protein from chicken liver: purification, characterization, and role of its prosthetic group, lipoic acid, in the glycine cleavage reaction. Arch Biochem Biophys 1979;197:454-62.
    • (1979) Arch Biochem Biophys , vol.197 , pp. 454-462
    • Fujiwara, K.1    Okamura, K.2    Motokawa, Y.3
  • 31
    • 0016194812 scopus 로고
    • Mechanism of the reversible glycine cleavage reaction in Arthrobacter globiformis. I. Purification and function of protein components required for the reaction
    • Kochi H, Kikuchi G. Mechanism of the reversible glycine cleavage reaction in Arthrobacter globiformis. I. Purification and function of protein components required for the reaction. J Biochem 1974;75:1113-27.
    • (1974) J Biochem , vol.75 , pp. 1113-1127
    • Kochi, H.1    Kikuchi, G.2
  • 32
    • 0017280254 scopus 로고
    • Mechanism of reversible glycine cleavage reaction in Arthrobacter globiformis. Function of lipoic acid in the cleavage and synthesis of glycine
    • Kochi H, Kikuchi G. Mechanism of reversible glycine cleavage reaction in Arthrobacter globiformis. Function of lipoic acid in the cleavage and synthesis of glycine. Arch Biochem Biophys 1976;173:71-81.
    • (1976) Arch Biochem Biophys , vol.173 , pp. 71-81
    • Kochi, H.1    Kikuchi, G.2
  • 33
    • 0014639028 scopus 로고
    • Glycine metabolism by rat liver mitochondria. IV. Isolation and characterization of hydrogen carrier protein, and essential factor forglycine metabolism
    • Motokawa Y, Kikuchi G. Glycine metabolism by rat liver mitochondria. IV. Isolation and characterization of hydrogen carrier protein, and essential factor for glycine metabolism. Arch Biochem Biophys 1969;135:402-9.
    • (1969) Arch Biochem Biophys , vol.135 , pp. 402-409
    • Motokawa, Y.1    Kikuchi, G.2
  • 34
    • 0014462309 scopus 로고
    • Glycine metabolism by rat liver mitochondria. II. Methylenetetrahy-drofolate as the direct one carbon donor in the reaction of glycine synthesis
    • Motokawa Y, Kikuchi G. Glycine metabolism by rat liver mitochondria. II. Methylene tetrahy-drofolate as the direct one carbon donor in the reaction of glycine synthesis. J Biochem 1969;65:71-5.
    • (1969) J Biochem , vol.65 , pp. 71-75
    • Motokawa, Y.1    Kikuchi, G.2
  • 35
    • 49949138663 scopus 로고
    • Further studies on the electron transport proteins involved in the oxidative decarboxylation of glycine
    • Baginsky ML, Huennekens FM. Further studies on the electron transport proteins involved in the oxidative decarboxylation of glycine. Arch Biochem Biophys 1967;120:703-11.
    • (1967) Arch Biochem Biophys , vol.120 , pp. 703-711
    • Baginsky, M.L.1    Huennekens, F.M.2
  • 36
    • 0014216045 scopus 로고
    • Glycine metabolism. III. A flavin-linked dehydrogenase associated with the glycine cleavage system in Peptococcus glycinophilus
    • Klein SM, Sagers RD. Glycine metabolism. III. A flavin-linked dehydrogenase associated with the glycine cleavage system in Peptococcus glycinophilus. J Biol Chem 1967;242:297-300.
    • (1967) J Biol Chem , vol.242 , pp. 297-300
    • Klein, S.M.1    Sagers, R.D.2
  • 37
    • 0028340511 scopus 로고
    • Acetoin catabolic system of Klebsiella pneumoniae CG43: Sequence, expression, and organization of the aco operon
    • Deng WL, Chang HY, Peng HL. Acetoin catabolic system of Klebsiella pneumoniae CG43: sequence, expression, and organization of the aco operon. J Bacteriol 1994;176:3527-35.
    • (1994) J Bacteriol , vol.176 , pp. 3527-3535
    • Deng, W.L.1    Chang, H.Y.2    Peng, H.L.3
  • 38
    • 0028157328 scopus 로고
    • Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
    • Oppermann FB, Steinbuchel A. Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J Bacteriol 1994;176:469-85.
    • (1994) J Bacteriol , vol.176 , pp. 469-485
    • Oppermann, F.B.1    Steinbuchel, A.2
  • 39
    • 0039478547 scopus 로고
    • Alpha-Ketoglutaric dehydrogenase. VI. Reversible oxidation of dihydrothioctamide by diphosphopyridine nucleotide
    • Sanadi DR, Langley M, Searls RL. alpha-Ketoglutaric dehydrogenase. VI. Reversible oxidation of dihydrothioctamide by diphosphopyridine nucleotide. J Biol Chem 1959;234:178-82.
    • (1959) J Biol Chem , vol.234 , pp. 178-182
    • Sanadi, D.R.1    Langley, M.2    Searls, R.L.3
  • 40
    • 0041370940 scopus 로고
    • The polarographic behavior of alpha-lipoic acid
    • Ke B. The polarographic behavior of alpha-lipoic acid. Biochim Biophys Acta 1957;25:650-1.
    • (1957) Biochim Biophys Acta , vol.25 , pp. 650-651
    • Ke, B.1
  • 41
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin TY, Kim PS. Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 1989;28:5282-7.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.Y.1    Kim, P.S.2
  • 42
    • 0025914427 scopus 로고
    • Pueyo de la Cuesta C, Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause G, Lundstrom J, Barea JL, Pueyo de la Cuesta C, Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J Biol Chem 1991;266:9494-500.
    • (1991) J Biol Chem , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3
  • 43
    • 0000961989 scopus 로고
    • Purification and properties of glutathione reductase of human erythrocytes
    • Scott EM, Duncan IW, Ekstrand V. Purification and properties of glutathione reductase of human erythrocytes. J Biol Chem 1963;238:3928-33.
    • (1963) J Biol Chem , vol.238 , pp. 3928-3933
    • Scott, E.M.1    Duncan, I.W.2    Ekstrand, V.3
  • 45
    • 0024562114 scopus 로고
    • Antioxidant activity of dihydrolipoate against microsomal lipid peroxidation and its dependence on alpha-tocopherol
    • Scholich H, Murphy ME, Sies H. Antioxidant activity of dihydrolipoate against microsomal lipid peroxidation and its dependence on alpha-tocopherol. Biochim Biophys Acta 1989;1001:256-61.
    • (1989) Biochim Biophys Acta , vol.1001 , pp. 256-261
    • Scholich, H.1    Murphy, M.E.2    Sies, H.3
  • 46
    • 0026778866 scopus 로고
    • Dihydrolipoic acid - a universal antioxidant both in the membrane and in the aqueous phase. Reduction of peroxyl, ascorbyl and chromanoxyl radicals
    • Kagan VE, Shvedova A, Serbinova E, et al. Dihydrolipoic acid - a universal antioxidant both in the membrane and in the aqueous phase. Reduction of peroxyl, ascorbyl and chromanoxyl radicals. Biochem Pharmacol 1992;44:1637-49.
    • (1992) Biochem Pharmacol , vol.44 , pp. 1637-1649
    • Kagan, V.E.1    Shvedova, A.2    Serbinova, E.3
  • 48
    • 0025369150 scopus 로고
    • Antioxidant effects of ubiquinones in microsomes and mitochondria are mediated by tocopherol recycling
    • Kagan V, Serbinova E, Packer L. Antioxidant effects of ubiquinones in microsomes and mitochondria are mediated by tocopherol recycling. Biochem Biophys Res Commun 1990;169:851-7.
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 851-857
    • Kagan, V.1    Serbinova, E.2    Packer, L.3
  • 51
    • 0027951044 scopus 로고
    • Effect of lipoic acid on redox state of coenzyme Q in mice treated with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and diethyldithiocarbamate
    • Gotz ME, Dirr A, Burger R, et al. Effect of lipoic acid on redox state of coenzyme Q in mice treated with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and diethyldithiocarbamate. Eur J Pharmacol 1994;266:291-300.
    • (1994) Eur J Pharmacol , vol.266 , pp. 291-300
    • Gotz, M.E.1    Dirr, A.2    Burger, R.3
  • 52
    • 0025031958 scopus 로고
    • Regulation of lipid peroxidation by glutathione and lipoic acid: Involvement of liver microsomal vitamin E free radical reductase
    • Bast A, Haenen GR. Regulation of lipid peroxidation by glutathione and lipoic acid: involvement of liver microsomal vitamin E free radical reductase. Adv Exp Med Biol 1990;264:111-6.
    • (1990) Adv Exp Med Biol , vol.264 , pp. 111-116
    • Bast, A.1    Haenen, G.R.2
  • 53
    • 0026356525 scopus 로고
    • Thioctic acid and dihydrolipoic acid are novel antioxidants which interact with reactive oxygen species
    • Suzuki YJ, Tsuchiya M, Packer L. Thioctic acid and dihydrolipoic acid are novel antioxidants which interact with reactive oxygen species. Free Radic Res Commun 1991;15:255-63.
    • (1991) Free Radic Res Commun , vol.15 , pp. 255-263
    • Suzuki, Y.J.1    Tsuchiya, M.2    Packer, L.3
  • 54
    • 0028345285 scopus 로고
    • Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation
    • Scott BC, Aruoma OI, Evans PJ, et al. Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation. Free Radic Res 1994;20:119-33.
    • (1994) Free Radic Res , vol.20 , pp. 119-133
    • Scott, B.C.1    Aruoma, O.I.2    Evans, P.J.3
  • 55
    • 0025949295 scopus 로고
    • Scavenging of hypochlorous acid by lipoic acid
    • Haenen GR, Bast A. Scavenging of hypochlorous acid by lipoic acid. Biochem Pharmacol 1991;42:2244-6.
    • (1991) Biochem Pharmacol , vol.42 , pp. 2244-2246
    • Haenen, G.R.1    Bast, A.2
  • 56
    • 0015946655 scopus 로고
    • The photoperoxidation of unsaturated organic molecules - IX. Lipoic acid inhibition of rubrene autoperoxidation
    • Stevens B, Perez SR, Small RD. The photoperoxidation of unsaturated organic molecules - IX. Lipoic acid inhibition of rubrene autoperoxidation. Photochem Photobiol 1974;19:315-16.
    • (1974) Photochem Photobiol , vol.19 , pp. 315-316
    • Stevens, B.1    Perez, S.R.2    Small, R.D.3
  • 57
    • 0027297705 scopus 로고
    • Antioxidant activities of dihydrolipoic acid and its structural homologues
    • Suzuki YJ, Tsuchiya M, Packer L. Antioxidant activities of dihydrolipoic acid and its structural homologues. Free Radic Res Commun 1993;18:115-22.
    • (1993) Free Radic Res Commun , vol.18 , pp. 115-122
    • Suzuki, Y.J.1    Tsuchiya, M.2    Packer, L.3
  • 58
    • 0025975753 scopus 로고
    • Singlet oxygen induced single-strand breaks in plasmid pBR322 DNA: The enhancing effect of thiols
    • Devasagayam TP, Di Mascio P, Kaiser S, Sies H. Singlet oxygen induced single-strand breaks in plasmid pBR322 DNA: the enhancing effect of thiols. Biochim Biophys Acta 1991;1088:409-12.
    • (1991) Biochim Biophys Acta , vol.1088 , pp. 409-412
    • Devasagayam, T.P.1    Di Mascio, P.2    Kaiser, S.3    Sies, H.4
  • 61
    • 0029909010 scopus 로고    scopus 로고
    • Neuroprotection by the metabolic antioxidant alpha-lipoic acid
    • Packer L, Tritschler HJ, Wessel K. Neuroprotection by the metabolic antioxidant alpha-lipoic acid. Free Radic Biol Med 1997;22:359-78.
    • (1997) Free Radic Biol Med , vol.22 , pp. 359-378
    • Packer, L.1    Tritschler, H.J.2    Wessel, K.3
  • 62
    • 84904599920 scopus 로고    scopus 로고
    • Activation of cytoprotective signaling pathways by alpha-lipoic acid
    • Patel MS, Packer L, eds., New York: CRC Press
    • Kiemer AK, Diesel B. Activation of cytoprotective signaling pathways by alpha-lipoic acid. In: Patel MS, Packer L, eds. Lipoic acid: energy production, antioxidant activity and health effects. New York: CRC Press; 2008:439-60.
    • (2008) Lipoic Acid: Energy Production, Antioxidant Activity and Health Effects , pp. 439-460
    • Kiemer, A.K.1    Diesel, B.2
  • 64
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998;16:225-60.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 66
    • 0026970404 scopus 로고
    • Nuclear factor kappa B: An oxidative stress-responsive transcription factor of eukaryotic cells (a review)
    • Schreck R, Albermann K, Baeuerle PA. Nuclear factor kappa B: an oxidative stress-responsive transcription factor of eukaryotic cells (a review). Free Radic Res Commun 1992;17:221-37.
    • (1992) Free Radic Res Commun , vol.17 , pp. 221-237
    • Schreck, R.1    Albermann, K.2    Baeuerle, P.A.3
  • 67
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, Hay RT. Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res 1992;20:3821-30.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 68
    • 0027076462 scopus 로고
    • Alpha-lipoic acid is a potent inhibitor of NF-kappa B activation in human T cells
    • Suzuki YJ, Aggarwal BB, Packer L. Alpha-lipoic acid is a potent inhibitor of NF-kappa B activation in human T cells. Biochem Biophys Res Commun 1992;189:1709-15.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1709-1715
    • Suzuki, Y.J.1    Aggarwal, B.B.2    Packer, L.3
  • 69
    • 0025787381 scopus 로고
    • Alpha-lipoic acid is an effective inhibitor of human immuno-deficiency virus (HIV-1) replication
    • Baur A, Harrer T, Peukert M, Jahn G, Kalden JR, Fleckenstein B. Alpha-lipoic acid is an effective inhibitor of human immuno-deficiency virus (HIV-1) replication. Klin Wochenschr 1991;69:722-4.
    • (1991) Klin Wochenschr , vol.69 , pp. 722-724
    • Baur, A.1    Harrer, T.2    Peukert, M.3    Jahn, G.4    Kalden, J.R.5    Fleckenstein, B.6
  • 71
    • 0030768236 scopus 로고    scopus 로고
    • The pharmacology of the antioxidant lipoic acid
    • Biewenga GP, Haenen GR, Bast A. The pharmacology of the antioxidant lipoic acid. Gen Pharmacol 1997;29:315-31.
    • (1997) Gen Pharmacol , vol.29 , pp. 315-331
    • Biewenga, G.P.1    Haenen, G.R.2    Bast, A.3
  • 72
    • 0002195204 scopus 로고    scopus 로고
    • An overview of lipoate chemistry
    • Fuchs J, Packer L, Zimmer G, eds., New York: Marcel Dekker
    • Biewenga GP, Haenen GRMM, Bast A. An overview of lipoate chemistry. In: Fuchs J, Packer L, Zimmer G, eds. Lipoic acid in health and disease. New York: Marcel Dekker; 1997:1-32.
    • (1997) Lipoic Acid in Health and Disease , pp. 1-32
    • Biewenga, G.P.1    Haenen, G.2    Bast, A.3
  • 73
    • 0033010474 scopus 로고    scopus 로고
    • Alpha-Lipoic acid decreases oxidative stress even in diabetic patients with poor glycemic control and albuminuria
    • Borcea V, Nourooz-Zadeh J, Wolff SP, et al. alpha-Lipoic acid decreases oxidative stress even in diabetic patients with poor glycemic control and albuminuria. Free Radic Biol Med 1999;26:1495-500.
    • (1999) Free Radic Biol Med , vol.26 , pp. 1495-1500
    • Borcea, V.1    Nourooz-Zadeh, J.2    Wolff, S.P.3
  • 74
    • 0032985492 scopus 로고    scopus 로고
    • Neuroprotective effects of alpha-lipoic acid and its positively charged amide analogue
    • Tirosh O, Sen CK, Roy S, Kobayashi MS, Packer L. Neuroprotective effects of alpha-lipoic acid and its positively charged amide analogue. Free Radic Biol Med 1999;26:1418-26.
    • (1999) Free Radic Biol Med , vol.26 , pp. 1418-1426
    • Tirosh, O.1    Sen, C.K.2    Roy, S.3    Kobayashi, M.S.4    Packer, L.5
  • 75
    • 0028821293 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: The lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
    • Morris TW, Reed KE, Cronan JE Jr. Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J Bacteriol 1995;177:1-10.
    • (1995) J Bacteriol , vol.177 , pp. 1-10
    • Morris, T.W.1    Reed, K.E.2    Cronan, J.E.3
  • 76
    • 26444504579 scopus 로고    scopus 로고
    • Function, attachment and synthesis of lipoic acid in Escherichia coli
    • Cronan JE Jr, Zhao X, Jiang Y. Function, attachment and synthesis of lipoic acid in Escherichia coli. Adv Microb Physiol 2005;50:103-46.
    • (2005) Adv Microb Physiol , vol.50 , pp. 103-146
    • Cronan, J.E.1    Zhao, X.2    Jiang, Y.3
  • 77
    • 84961044156 scopus 로고
    • Studies on a lipoic acid-activating system
    • Reed LJ, Leach FR, Koike M. Studies on a lipoic acid-activating system. J Biol Chem 1958;232:123-42.
    • (1958) J Biol Chem , vol.232 , pp. 123-142
    • Reed, L.J.1    Leach, F.R.2    Koike, M.3
  • 78
    • 0028247161 scopus 로고
    • Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product
    • Morris TW, Reed KE, Cronan JE Jr. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. J Biol Chem 1994;269:16091-100.
    • (1994) J Biol Chem , vol.269 , pp. 16091-16100
    • Morris, T.W.1    Reed, K.E.2    Cronan, J.E.3
  • 79
    • 0029148130 scopus 로고
    • Purification and properties of the lipoate protein ligase of Escherichia coli
    • Green DE, Morris TW, Green J, Cronan JE Jr, Guest JR. Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem J 1995;309:853-62.
    • (1995) Biochem J , vol.309 , pp. 853-862
    • Green, D.E.1    Morris, T.W.2    Green, J.3    Cronan, J.E.4    Guest, J.R.5
  • 80
    • 0028244665 scopus 로고
    • Purification and characterization of lipoyl-AMP:NMysine lipoyltransferase from bovine liver mitochondria
    • Fujiwara K, Okamura-Ikeda K, Motokawa Y. Purification and characterization of lipoyl-AMP:NMysine lipoyltransferase from bovine liver mitochondria. J Biol Chem 1994;269:16605-9.
    • (1994) J Biol Chem , vol.269 , pp. 16605-16609
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 81
    • 0035800735 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver
    • Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y. Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J Biol Chem 2001;276:28819-23.
    • (2001) J Biol Chem , vol.276 , pp. 28819-28823
    • Fujiwara, K.1    Takeuchi, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4
  • 82
    • 77952915341 scopus 로고    scopus 로고
    • Lipoic acid metabolism in microbial pathogens
    • Spalding MD, Prigge ST. Lipoic acid metabolism in microbial pathogens. Microbiol Mol Biol Rev 2010;74:200-28.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 200-228
    • Spalding, M.D.1    Prigge, S.T.2
  • 83
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acylcarrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan SW, Cronan JE Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J Biol Chem 1997;272:17903-6.
    • (1997) J Biol Chem , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan, J.E.2
  • 84
    • 0030925929 scopus 로고    scopus 로고
    • Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae
    • Brody S, Oh C, Schweizer UHE. Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae. FEBS Lett 1997;408:217-20.
    • (1997) FEBS Lett , vol.408 , pp. 217-220
    • Brody, S.1    Oh, C.2    Schweizer, U.H.E.3
  • 85
    • 0348229020 scopus 로고    scopus 로고
    • Assembly of the covalent linkage between lipoic acid and its cognate enzymes
    • Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE Jr. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol 2003;10:1293-302.
    • (2003) Chem Biol , vol.10 , pp. 1293-1302
    • Zhao, X.1    Miller, J.R.2    Jiang, Y.3    Marletta, M.A.4    Cronan, J.E.5
  • 86
    • 29244461444 scopus 로고    scopus 로고
    • The reaction of LipB, the octanoyl-[acyl carrier protein]:Protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate
    • Zhao X, Miller JR, Cronan JE Jr. The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate. Biochemistry 2005;44:16737-46.
    • (2005) Biochemistry , vol.44 , pp. 16737-16746
    • Zhao, X.1    Miller, J.R.2    Cronan, J.E.3
  • 87
    • 11844282751 scopus 로고    scopus 로고
    • Expression, purification, and physical characterization of Escherichia coli lipoyl(Octanoyl)transferase
    • Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, et al. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr Purif 2005;39:269-82.
    • (2005) Protein Expr Purif , vol.39 , pp. 269-282
    • Nesbitt, N.M.1    Baleanu-Gogonea, C.2    Cicchillo, R.M.3
  • 88
    • 2542641045 scopus 로고    scopus 로고
    • Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid
    • Cicchillo RM, Iwig DF, Jones AD, et al. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry 2004;43:6378-86.
    • (2004) Biochemistry , vol.43 , pp. 6378-6386
    • Cicchillo, R.M.1    Iwig, D.F.2    Jones, A.D.3
  • 89
    • 33747285132 scopus 로고    scopus 로고
    • Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner
    • Douglas P, Kriek M, Bryant P, Roach PL. Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner. Angew Chem Int Ed Engl 2006;45:5197-9.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5197-5199
    • Douglas, P.1    Kriek, M.2    Bryant, P.3    Roach, P.L.4
  • 91
    • 79954422712 scopus 로고    scopus 로고
    • A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
    • Christensen QH, Martin N, Mansilla MC, de Mendoza D, Cronan JE Jr. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol Microbiol 2011;80:350-63.
    • (2011) Mol Microbiol , vol.80 , pp. 350-363
    • Christensen, Q.H.1    Martin, N.2    Mansilla, M.C.3    De Mendoza, D.4    Cronan, J.E.5
  • 92
    • 79954414898 scopus 로고    scopus 로고
    • A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
    • Martin N, Christensen QH, Mansilla MC, Cronan JE Jr, de Mendoza D. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol Microbiol 2011;80:335-49.
    • (2011) Mol Microbiol , vol.80 , pp. 335-349
    • Martin, N.1    Christensen, Q.H.2    Mansilla, M.C.3    Cronan, J.E.4    De Mendoza, D.5
  • 93
    • 78649299811 scopus 로고    scopus 로고
    • Lipoic acid synthesis: A new family of octanoyltransferases generally annotated as lipoate protein ligases
    • Christensen QH, Cronan JE Jr. Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases. Biochemistry 2010;49:10024-36.
    • (2010) Biochemistry , vol.49 , pp. 10024-10036
    • Christensen, Q.H.1    Cronan, J.E.2
  • 94
    • 0014344705 scopus 로고
    • Biochemical and genetic studies with lysine + methionine mutants of Escherichia coli: Lipoic acid and a-ketoglutarate dehydrogenase-less mutants
    • Herbert AA, Guest JR. Biochemical and genetic studies with lysine + methionine mutants of Escherichia coli: lipoic acid and a-ketoglutarate dehydrogenase-less mutants. J Gen Microbiol 1968;53:363-81.
    • (1968) J Gen Microbiol , vol.53 , pp. 363-381
    • Herbert, A.A.1    Guest, J.R.2
  • 95
    • 0026668860 scopus 로고
    • The biosynthesis of lipoic acid: Cloning of lip, a lipoate biosynthetic locus of Escherichia coli
    • Hayden MA, Huang I, Bussiere DE, Ashley GW. The biosynthesis of lipoic acid: cloning of lip, a lipoate biosynthetic locus of Escherichia coli. J Biol Chem 1992;267:9512-5.
    • (1992) J Biol Chem , vol.267 , pp. 9512-9515
    • Hayden, M.A.1    Huang, I.2    Bussiere, D.E.3    Ashley, G.W.4
  • 96
    • 0027401765 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: Sequencing and functional characterization of the lipA and lipB genes
    • Reed KE, Cronan JE Jr. Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. J Bacteriol 1993;175:1325-36.
    • (1993) J Bacteriol , vol.175 , pp. 1325-1336
    • Reed, K.E.1    Cronan, J.E.2
  • 98
    • 0000300645 scopus 로고
    • Biosynthesis of lipoic acid. 1. Incorporation of specifically tritiated octanoic acid into lipoic acid
    • Parry RJ. Biosynthesis of lipoic acid. 1. Incorporation of specifically tritiated octanoic acid into lipoic acid. J Am Chem Soc 1977;99:6464-6.
    • (1977) J am Chem Soc , vol.99 , pp. 6464-6466
    • Parry, R.J.1
  • 99
    • 0001179909 scopus 로고
    • Biosynthesis of lipoic acid. 2. Stereochemistry of sulfur introduction at C-6 of octanoic acid
    • Parry RJ, Trainor DA. Biosynthesis of lipoic acid. 2. Stereochemistry of sulfur introduction at C-6 of octanoic acid. J Am Chem Soc 1978;100:5243-4.
    • (1978) J am Chem Soc , vol.100 , pp. 5243-5244
    • Parry, R.J.1    Trainor, D.A.2
  • 100
    • 0018875796 scopus 로고
    • Stable isotope studies on the biosynthesis of lipoic acid in Escherichia coli
    • White RH. Stable isotope studies on the biosynthesis of lipoic acid in Escherichia coli. Biochemistry 1980;19:15-9.
    • (1980) Biochemistry , vol.19 , pp. 15-19
    • White, R.H.1
  • 101
    • 0018841201 scopus 로고
    • Stoichiometry and stereochemistry of deuterium incorporated into fatty acids by cells of Escherichia coli grown on [methyl-2H3]acetate
    • 3]acetate. Biochemistry 1980;19:9-15.
    • (1980) Biochemistry , vol.19 , pp. 9-15
    • White, R.H.1
  • 102
    • 33847086495 scopus 로고
    • Biosynthesis of lipoic acid: Extent of incorporation of deuterated hydroxy- and thiooctanoic acids into lipoic acid
    • White RH. Biosynthesis of lipoic acid: extent of incorporation of deuterated hydroxy- and thiooctanoic acids into lipoic acid. J Am Chem Soc 1980;102:6605-7.
    • (1980) J am Chem Soc , vol.102 , pp. 6605-6607
    • White, R.H.1
  • 103
    • 0000386636 scopus 로고
    • Biosynthesis of some sulfur-containing natural products investigations of the mechanism of carbon-sulfur bond formation
    • Parry RJ. Biosynthesis of some sulfur-containing natural products investigations of the mechanism of carbon-sulfur bond formation. Tetrahedron 1983;39:1215-38.
    • (1983) Tetrahedron , vol.39 , pp. 1215-1238
    • Parry, R.J.1
  • 104
    • 0027157794 scopus 로고
    • Biosynthesis of lipoic acid: Characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9
    • Hayden MA, Huang IY, Iliopoulos G, Orozco M, Ashley GW. Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9. Biochemistry 1993;32:3778-82.
    • (1993) Biochemistry , vol.32 , pp. 3778-3782
    • Hayden, M.A.1    Huang, I.Y.2    Iliopoulos, G.3    Orozco, M.4    Ashley, G.W.5
  • 106
    • 0345120596 scopus 로고    scopus 로고
    • The lipoate synthase from Escherichia coli is an iron-sulfur protein
    • Ollagnier-de Choudens S, Fontecave M. The lipoate synthase from Escherichia coli is an iron-sulfur protein. FEBS Lett 1999;453:25-8.
    • (1999) FEBS Lett , vol.453 , pp. 25-28
    • Ollagnier-De Choudens, S.1    Fontecave, M.2
  • 107
  • 108
  • 109
    • 0023645851 scopus 로고
    • The role of S-adenosylmethionine in the lysine 2,3-aminomutase reaction
    • Moss M, Frey PA. The role of S-adenosylmethionine in the lysine 2,3-aminomutase reaction. J Biol Chem 1987;262:14859-62.
    • (1987) J Biol Chem , vol.262 , pp. 14859-14862
    • Moss, M.1    Frey, P.A.2
  • 110
    • 0024496311 scopus 로고
    • Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
    • Baraniak J, Moss ML, Frey PA. Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine. J Biol Chem 1989;264:1357-60.
    • (1989) J Biol Chem , vol.264 , pp. 1357-1360
    • Baraniak, J.1    Moss, M.L.2    Frey, P.A.3
  • 112
    • 84866018235 scopus 로고    scopus 로고
    • Radical SAM enzymes and radical enzymology
    • Booker SJ. Radical SAM enzymes and radical enzymology. Biochim Biophys Acta 2012;1824: 1151-3.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 1151-1153
    • Booker, S.J.1
  • 113
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer G, Moser J, Heinz DW, Jahn D, Schubert WD. Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J 2003;22:6214-24.
    • (2003) EMBO J , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 114
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 2004;303:76-9.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 115
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • Hanzelmann P, Schindelin H. Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc Natl Acad Sci USA 2004;101:12870-5.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12870-12875
    • Hanzelmann, P.1    Schindelin, H.2
  • 116
    • 25444494469 scopus 로고    scopus 로고
    • The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
    • Lepore BW, Ruzicka FJ, Frey PA, Ringe D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proc Natl Acad Sci USA 2005;102:13819-24.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13819-13824
    • Lepore, B.W.1    Ruzicka, F.J.2    Frey, P.A.3    Ringe, D.4
  • 117
    • 9744258825 scopus 로고    scopus 로고
    • The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase
    • Jarrett JT. The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase. Arch Biochem Biophys 2005;433:312-21.
    • (2005) Arch Biochem Biophys , vol.433 , pp. 312-321
    • Jarrett, J.T.1
  • 119
    • 34548504334 scopus 로고    scopus 로고
    • Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA
    • Suzuki Y, Noma A, Suzuki T, et al. Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA. J Mol Biol 2007;372:1204-14.
    • (2007) J Mol Biol , vol.372 , pp. 1204-1214
    • Suzuki, Y.1    Noma, A.2    Suzuki, T.3
  • 120
    • 49649115936 scopus 로고    scopus 로고
    • X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima
    • Nicolet Y, Rubach JK, Posewitz MC, et al. X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima. J Biol Chem 2008;283:18861-72.
    • (2008) J Biol Chem , vol.283 , pp. 18861-18872
    • Nicolet, Y.1    Rubach, J.K.2    Posewitz, M.C.3
  • 121
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
    • Miller JR, Busby RW, Jordan SW, et al. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 2000;39:15166-78.
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2    Jordan, S.W.3
  • 122
    • 33644944475 scopus 로고    scopus 로고
    • The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate
    • Bryant P, Kriek M, Wood RJ, Roach PL. The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate. Anal Biochem 2006;351:44-9.
    • (2006) Anal Biochem , vol.351 , pp. 44-49
    • Bryant, P.1    Kriek, M.2    Wood, R.J.3    Roach, P.L.4
  • 123
    • 78650238422 scopus 로고    scopus 로고
    • Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism
    • Parveen N, Cornell KA. Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism. Mol Microbiol 2011;79:7-20.
    • (2011) Mol Microbiol , vol.79 , pp. 7-20
    • Parveen, N.1    Cornell, K.A.2
  • 124
    • 19544377011 scopus 로고    scopus 로고
    • A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase
    • Choi-Rhee E, Cronan JE Jr. A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase. Chem Biol 2005;12:589-93.
    • (2005) Chem Biol , vol.12 , pp. 589-593
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 125
    • 64049108275 scopus 로고    scopus 로고
    • Product inhibition in the radical S-adenosylme-thionine family
    • Challand MR, Ziegert T, Douglas P, et al. Product inhibition in the radical S-adenosylme-thionine family. FEBS Lett 2009;583:1358-62.
    • (2009) FEBS Lett , vol.583 , pp. 1358-1362
    • Challand, M.R.1    Ziegert, T.2    Douglas, P.3
  • 126
    • 0037719823 scopus 로고    scopus 로고
    • Effect of iron-sulfur cluster assembly proteins on the expression of Escherichia coli lipoic acid synthase
    • Kriek M, Peters L, Takahashi Y, Roach PL. Effect of iron-sulfur cluster assembly proteins on the expression of Escherichia coli lipoic acid synthase. Protein Expr Purif 2003;28:241-5.
    • (2003) Protein Expr Purif , vol.28 , pp. 241-245
    • Kriek, M.1    Peters, L.2    Takahashi, Y.3    Roach, P.L.4
  • 128
    • 34147189950 scopus 로고    scopus 로고
    • Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems
    • Dos Santos P, Johnson D, Ragle B, Unciuleac M, Dean D. Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. J Bacteriol 2007;189:2854-62.
    • (2007) J Bacteriol , vol.189 , pp. 2854-2862
    • Dos Santos, P.1    Johnson, D.2    Ragle, B.3    Unciuleac, M.4    Dean, D.5
  • 129
    • 33750445986 scopus 로고    scopus 로고
    • Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii
    • Johnson DC, Unciuleac M-C, Dean DR. Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii. J Bacteriol 2006;188:7551-61.
    • (2006) J Bacteriol , vol.188 , pp. 7551-7561
    • Johnson, D.C.1    Unciuleac, M.-C.2    Dean, D.R.3
  • 131
    • 0141620318 scopus 로고    scopus 로고
    • Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the (4Fe-4S) center in lysine 2,3-aminomutase
    • Chen D, Walsby C, Hoffman BM, Frey PA. Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the (4Fe-4S) center in lysine 2,3-aminomutase. J Am Chem Soc 2003;125:11788-9.
    • (2003) J am Chem Soc , vol.125 , pp. 11788-11789
    • Chen, D.1    Walsby, C.2    Hoffman, B.M.3    Frey, P.A.4
  • 132
    • 0037181351 scopus 로고    scopus 로고
    • Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active (4Fe-4S)+ cluster of pyruvate formate-lyase activating enzyme
    • Walsby CJ, Hong W, Broderick WE, et al. Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active (4Fe-4S)+ cluster of pyruvate formate-lyase activating enzyme. J Am Chem Soc 2002;124:3143-51.
    • (2002) J am Chem Soc , vol.124 , pp. 3143-3151
    • Walsby, C.J.1    Hong, W.2    Broderick, W.E.3
  • 133
    • 0037065661 scopus 로고    scopus 로고
    • Coordination of adenosylme-thionine to a unique iron site of the (4Fe-4S) of pyruvate formate-lyase activating enzyme: A Mossbauer spectroscopic study
    • Krebs C, Broderick WE, Henshaw TF, Broderick JB, Huynh BH. Coordination of adenosylme-thionine to a unique iron site of the (4Fe-4S) of pyruvate formate-lyase activating enzyme: a Mossbauer spectroscopic study. J Am Chem Soc 2002;124:912-3.
    • (2002) J am Chem Soc , vol.124 , pp. 912-913
    • Krebs, C.1    Broderick, W.E.2    Henshaw, T.F.3    Broderick, J.B.4    Huynh, B.H.5
  • 134
    • 0038648509 scopus 로고    scopus 로고
    • Structural studies of the interaction of S-adenosylme-thionine with the [4Fe-4S] clusters in biotin synthase and pyruvate formate-lyase activating enzyme
    • Cosper MM, Cosper NJ, Hong W, et al. Structural studies of the interaction of S-adenosylme-thionine with the [4Fe-4S] clusters in biotin synthase and pyruvate formate-lyase activating enzyme. Protein Sci 2003;12:1573-7.
    • (2003) Protein Sci , vol.12 , pp. 1573-1577
    • Cosper, M.M.1    Cosper, N.J.2    Hong, W.3
  • 135
    • 36048929198 scopus 로고    scopus 로고
    • Binding energy in the one-electron reductive cleavage of S-adenosylme-thionine in lysine 2,3-aminomutase, a radical SAM enzyme
    • Wang SC, Frey PA. Binding energy in the one-electron reductive cleavage of S-adenosylme-thionine in lysine 2,3-aminomutase, a radical SAM enzyme. Biochemistry 2007;46:12889-95.
    • (2007) Biochemistry , vol.46 , pp. 12889-12895
    • Wang, S.C.1    Frey, P.A.2
  • 136
    • 33644860151 scopus 로고    scopus 로고
    • Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase
    • 2+/1+ in lysine 2,3-aminomutase. Biochemistry 2006;45:3219-25.
    • (2006) Biochemistry , vol.45 , pp. 3219-3225
    • Hinckley, G.T.1    Frey, P.A.2
  • 137
    • 0010219797 scopus 로고
    • Polarography of sulfonium salts
    • Colichman EL, Love DL. Polarography of sulfonium salts. J Org Chem 1952;18:40-6.
    • (1952) J Org Chem , vol.18 , pp. 40-46
    • Colichman, E.L.1    Love, D.L.2
  • 138
    • 0021464427 scopus 로고
    • Mechanism of one-electron electrochemical reductive cleavage reactions of sulfonium salts
    • Saeva FD, Morgan BP. Mechanism of one-electron electrochemical reductive cleavage reactions of sulfonium salts. J Am Chem Soc 1984;106:4121-5.
    • (1984) J am Chem Soc , vol.106 , pp. 4121-4125
    • Saeva, F.D.1    Morgan, B.P.2
  • 139
    • 0032748442 scopus 로고    scopus 로고
    • Spectroscopic evidence for the participation of an allylic analogue of the 5'-deoxyadenosyl radical in the reaction of lysine 2,3-aminomutase
    • Magnusson OT, Reed GH, Frey PA. Spectroscopic evidence for the participation of an allylic analogue of the 5'-deoxyadenosyl radical in the reaction of lysine 2,3-aminomutase. J Am Chem Soc 1999;121:9764-5.
    • (1999) J am Chem Soc , vol.121 , pp. 9764-9765
    • Magnusson, O.T.1    Reed, G.H.2    Frey, P.A.3
  • 140
    • 0035800077 scopus 로고    scopus 로고
    • Characterization of an allylic analogue of the 5'-deoxyadenosyl radical: An intermediate in the reaction of lysine 2,3-aminomutase
    • Magnusson OT, Reed GH, Frey PA. Characterization of an allylic analogue of the 5'-deoxyadenosyl radical: an intermediate in the reaction of lysine 2,3-aminomutase. Biochemistry 2001;40:7773-82.
    • (2001) Biochemistry , vol.40 , pp. 7773-7782
    • Magnusson, O.T.1    Reed, G.H.2    Frey, P.A.3
  • 141
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • Cicchillo RM, Booker SJ. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J Am Chem Soc 2005;127:2860-1.
    • (2005) J am Chem Soc , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 142
  • 143


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.