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Volumn 45, Issue 10, 2006, Pages 3219-3225

Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; ELECTROCHEMISTRY; FREE RADICAL POLYMERIZATION; IRON; REDUCTION; SUBSTRATES;

EID: 33644860151     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0519497     Document Type: Article
Times cited : (50)

References (38)
  • 2
    • 0000489779 scopus 로고
    • Importance of organic radicals in enzymatic cleavage of unactivated C-H Bonds
    • Frey, P. A. (1990) Importance of Organic Radicals in Enzymatic Cleavage of Unactivated C-H Bonds, Chem. Rev. 90, 1343-1357.
    • (1990) Chem. Rev. , vol.90 , pp. 1343-1357
    • Frey, P.A.1
  • 3
    • 0032562217 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance
    • Lieder, K. W., Booker, S., Ruzicka, F. J., Beinert, H., Reed, G. H., and Frey, P. A. (1998) S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-aminomutase and Observation of the Catalytically Functional Iron-Sulfur Centers by Electron Paramagnetic Resonance, Biochemistry 37, 2578-2585.
    • (1998) Biochemistry , vol.37 , pp. 2578-2585
    • Lieder, K.W.1    Booker, S.2    Ruzicka, F.J.3    Beinert, H.4    Reed, G.H.5    Frey, P.A.6
  • 4
    • 0031577321 scopus 로고    scopus 로고
    • Biotin synthase, a new member of the familiy of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical
    • Guianvarc'h, D., Florentin, D., Bui, B. T. S., Nunzi, F., and Marquet, A. (1997) Biotin Synthase, a New Member of the Familiy of Enzymes Which Uses S-Adenosylmethionine as a Source of Deoxyadenosyl Radical, Biochem. Biophys. Res. Commun. 236, 402-406.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 402-406
    • Guianvarc'H, D.1    Florentin, D.2    Bui, B.T.S.3    Nunzi, F.4    Marquet, A.5
  • 5
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a Lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from ocatnoyl-acyl carrier protein
    • Miller, J. R., Busby, R. W., Jordan, S. W., Cheek, J., Henshaw, T. F., and Ashley, G. W. (2000) Escherichia coli LipA is a Lipoyl Synthase: In Vitro Biosynthesis of Lipoylated Pyruvate Dehydrogenase Complex from Ocatnoyl-Acyl Carrier Protein, Biochemistry 39, 15166-15178.
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2    Jordan, S.W.3    Cheek, J.4    Henshaw, T.F.5    Ashley, G.W.6
  • 7
    • 0034734328 scopus 로고    scopus 로고
    • 1+ cluster of pyruvate formate-lyase activating enzyme generates the glycyl radical on pyruvate formate-lyase: EPR-detected single
    • 1+ Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single, J. Am. Chem. Soc. 122, 8331-8332.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8331-8332
    • Henshaw, T.F.1    Cheek, J.2    Broderick, J.B.3
  • 8
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar bisynthetic pathways with radical mechanisms: Functional characterization
    • Sofia, H. J., Chen, G., Hetzler, B. G., Reyes-Spindola, J. F., and Miller, N. E. (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar bisynthetic pathways with radical mechanisms: Functional characterization, Nucleic Acids Res. 29, 1097-1106.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 9
    • 0034841061 scopus 로고    scopus 로고
    • Adenosylmethionine-dependent iron-sulfur enzymes: Versatile clusters in a radical new role
    • Cheek, J., and Broderick, J. B. (2001) Adenosylmethionine-dependent iron-sulfur enzymes: Versatile clusters in a radical new role, J. Biol. Inorg. Chem. 6, 209-226.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 209-226
    • Cheek, J.1    Broderick, J.B.2
  • 11
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • Flint, D. H., and Allen, R. M. (1996) Iron-Sulfur Proteins with Nonredox Functions, Chem. Rev. 96, 2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 12
    • 0026483949 scopus 로고
    • Characterization of iron sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy
    • Petrovich, R. M., Ruzicka, F. J., Reed, G. H., and Frey, P. A. (1992) Characterization of Iron Sulfur Clusters in Lysine 2,3-Aminomutase by Electron Paramagnetic Resonance Spectroscopy, Biochemistry 31, 10774-10781.
    • (1992) Biochemistry , vol.31 , pp. 10774-10781
    • Petrovich, R.M.1    Ruzicka, F.J.2    Reed, G.H.3    Frey, P.A.4
  • 13
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in Biology
    • Holm, R. H., Kennepohl, P., and Solomon, E. I. (1996) Structural and Functional Aspects of Metal Sites in Biology, Chem. Rev. 96, 2239-2314.
    • (1996) Chem. Rev. , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 14
    • 0034719099 scopus 로고    scopus 로고
    • Direct FeS cluster involvement in generation of a radical in Lysine 2,3-Aminomutase
    • Cosper, N. J., Booker, S., Ruzicka, F. J., Frey, P. A., and Scott, R. A. (2000) Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase, Biochemistry 39, 15668-15673.
    • (2000) Biochemistry , vol.39 , pp. 15668-15673
    • Cosper, N.J.1    Booker, S.2    Ruzicka, F.J.3    Frey, P.A.4    Scott, R.A.5
  • 15
    • 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, B. M., and Frey, P. A. (2003) Coordination and Mechanism of Reversible Cleavage of S-Adenosylmethionine by the [4Fe-4S] Center in Lysine 2,3-Aminomutase, J. Am. Chem. Soc. 125, 11788-11789.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11788-11789
    • Chen, D.1    Walsby, C.2    Hoffman, B.M.3    Frey, P.A.4
  • 16
    • 0002477071 scopus 로고    scopus 로고
    • Radical intermediates in the reaction of Lysine 2,3-aminomutase
    • Frey, P. A., and Booker, S. (1999) Radical Intermediates in the Reaction of Lysine 2,3-aminomutase, Adv. Free Radical Chem. 2, 1-43.
    • (1999) Adv. Free Radical Chem. , vol.2 , pp. 1-43
    • Frey, P.A.1    Booker, S.2
  • 17
    • 0010219797 scopus 로고
    • Polarography of sulfonium salts
    • Colichman, E. L., and Love, D. L. (1953) Polarography of Sulfonium Salts, J. Org. Chem. 18, 40-46.
    • (1953) J. Org. Chem. , vol.18 , pp. 40-46
    • Colichman, E.L.1    Love, D.L.2
  • 18
    • 0033214318 scopus 로고    scopus 로고
    • Synthesis of two stable nitrogen analogues of S-Adenosyl-L-methionine
    • Thompson, M. J., Mekhalfia, A., Hornby, D. P., and Blackburn, G. M. (1999) Synthesis of Two Stable Nitrogen Analogues of S-Adenosyl-L-methionine, J. Org. Chem. 64, 7467-7473.
    • (1999) J. Org. Chem. , vol.64 , pp. 7467-7473
    • Thompson, M.J.1    Mekhalfia, A.2    Hornby, D.P.3    Blackburn, G.M.4
  • 19
    • 14444267725 scopus 로고
    • The electrochemical properties of three dypyridinium salts as mediators
    • Salmon, R. T., and Hawkridge, F. M. (1980) The Electrochemical Properties of Three Dypyridinium Salts as Mediators, J. Electroanal. Chem. 112, 253-364.
    • (1980) J. Electroanal. Chem. , vol.112 , pp. 253-364
    • Salmon, R.T.1    Hawkridge, F.M.2
  • 20
    • 0033988966 scopus 로고    scopus 로고
    • Lysine 2,3-Aminomutase from Closlridium subterminale SB4: Mass spectral chacterization of cyanogen bromide-treated peptides and cloning
    • Ruzicka, F. J., Lieder, K. W., and Frey, P. A. (2000) Lysine 2,3-Aminomutase from Closlridium subterminale SB4: Mass Spectral Chacterization of Cyanogen Bromide-Treated Peptides and Cloning, J. Bacteriol. 182, 469-476.
    • (2000) J. Bacteriol. , vol.182 , pp. 469-476
    • Ruzicka, F.J.1    Lieder, K.W.2    Frey, P.A.3
  • 21
    • 0025119601 scopus 로고    scopus 로고
    • Activation of Lysine 2,3-Aminomutase by S-Adenosylmethionine
    • (1-990)
    • Moss, M. L., and Frey, P. A. (1-990) Activation of Lysine 2,3-Aminomutase by S-Adenosylmethionine, J. Biol. Chem. 265, 18112-18115.
    • J. Biol. Chem. , vol.265 , pp. 18112-18115
    • Moss, M.L.1    Frey, P.A.2
  • 24
    • 0021686102 scopus 로고
    • Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase
    • Kennedy, M. C., Kent, T. A., Emptage, M., Merkle, H., Beinert, H., and Munck, E. (1984) Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase, J. Biol. Chem. 259, 14463-14471.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14463-14471
    • Kennedy, M.C.1    Kent, T.A.2    Emptage, M.3    Merkle, H.4    Beinert, H.5    Munck, E.6
  • 25
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert, H. (1983) Semi-micro Methods for Analysis of Labile Sulfide and of Labile Sulfide plus Sulfane Sulfur in Unusually Stable Iron-Sulfur Proteins, Anal. Biochem. 131, 373-378.
    • (1983) Anal. Biochem. , vol.131 , pp. 373-378
    • Beinert, H.1
  • 26
    • 0035866571 scopus 로고    scopus 로고
    • Inhibition of Lysine 2,3-Aminomutase by the alternative substrate 4-Thialysine and characterization of the 4-Thialysyl radical intermediate
    • Miller, J., Bandarian, V., Reed, G. H., and Frey, P. A. (2001) Inhibition of Lysine 2,3-Aminomutase by the Alternative Substrate 4-Thialysine and Characterization of the 4-Thialysyl Radical Intermediate, Arch. Biochem. Biophys. 387, 281-288.
    • (2001) Arch. Biochem. Biophys. , vol.387 , pp. 281-288
    • Miller, J.1    Bandarian, V.2    Reed, G.H.3    Frey, P.A.4
  • 27
    • 31144439751 scopus 로고    scopus 로고
    • Construction of a spectroelectrochemical titrator adaptable to multiple spectroscopies
    • Hinckley, G., and Frey, P. A. (2006) Construction of a Spectroelectrochemical Titrator Adaptable to Multiple Spectroscopies, Anal. Biochem. 349, 103-111.
    • (2006) Anal. Biochem. , vol.349 , pp. 103-111
    • Hinckley, G.1    Frey, P.A.2
  • 30
    • 0015835755 scopus 로고
    • Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide
    • Cammack, R. (1973) "Super-Reduction" of Chromatium High-Potential Iron-Sulphur Protein in the Presence of Dimethyl Sulphoxide, Biochem. Biophys. Res. Commun. 54, 548-554.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 548-554
    • Cammack, R.1
  • 31
    • 0029088950 scopus 로고
    • Reversible super-reduction of the cubane [4Fe-4S]-(3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies
    • Heering, H. A., Bulsink, Y. B. M., Hagen, W. R., and Meyer, T. E. (1995) Reversible super-reduction of the cubane [4Fe-4S]-(3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies, Eur. J. Biochem. 232, 811-817.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 811-817
    • Heering, H.A.1    Bulsink, Y.B.M.2    Hagen, W.R.3    Meyer, T.E.4
  • 34
    • 0035805656 scopus 로고    scopus 로고
    • 2-/3- clusters with sulfonium cations: Analogue reaction systems for the initial step in biotin synthase catalysis
    • 2-/3- Clusters with Sulfonium Cations: Analogue Reaction Systems for the Initial Step in Biotin Synthase Catalysis, Inorg. Chem. 40, 2785-2793.
    • (2001) Inorg. Chem. , vol.40 , pp. 2785-2793
    • Daley, C.J.A.1    Holm, R.H.2
  • 35
    • 0023645851 scopus 로고
    • The role of S-Adenosylmethionine in the Lysine 2,3-aminomutase reaction
    • Moss, M. L., and Frey, P. A. (1987) The Role of S-Adenosylmethionine in the Lysine 2,3-aminomutase Reaction, J. Biol. Chem. 262, 14859-14862.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14859-14862
    • Moss, M.L.1    Frey, P.A.2
  • 36
    • 0035800077 scopus 로고    scopus 로고
    • Characterization of an allylic analouge of the 5′-deoxyadenosyl radical: An intermediate in the reaction of Lyisne 2,3-Aminomutase
    • Magnusson, O. T., Reed, G. H., and Frey, P. A. (2001) Characterization of an Allylic Analouge of the 5′-Deoxyadenosyl Radical: An Intermediate in the Reaction of Lyisne 2,3-Aminomutase, Biochemistry 40, 7773-7782.
    • (2001) Biochemistry , vol.40 , pp. 7773-7782
    • Magnusson, O.T.1    Reed, G.H.2    Frey, P.A.3
  • 37
    • 0000415615 scopus 로고    scopus 로고
    • Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins
    • Capozzi, F., Ciurli, S., and Luchinat, C. (1998) Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins, Struct. Bonding 90, 127-160.
    • (1998) Struct. Bonding , vol.90 , pp. 127-160
    • Capozzi, F.1    Ciurli, S.2    Luchinat, C.3
  • 38
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • Ugulava, N. B., Gibney, R. R., and Jarrett, J. T. (2001) Biotin Synthase Contains Two Distinct Iron-Sulfur Cluster Binding Sites: Chemical and Spectroelectrochemical Analysis of Iron-Sulfur Cluster Interconversions. Biochemistry 40, 8343-8351.
    • (2001) Biochemistry , vol.40 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, R.R.2    Jarrett, J.T.3


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