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Volumn 1853, Issue 6, 2015, Pages 1395-1405

Mössbauer spectroscopy of Fe/S proteins

Author keywords

EPR spectroscopy; Fe S clusters; Mossbauer spectroscopy

Indexed keywords

IRON; IRON SULFUR PROTEIN; SULFUR;

EID: 84937107667     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.12.005     Document Type: Review
Times cited : (104)

References (103)
  • 1
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 2000, 5:2-15.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 2
    • 0344834199 scopus 로고
    • Iron-sulfur clusters in enzymes - themes and variations
    • Cammack R. Iron-sulfur clusters in enzymes - themes and variations. Adv. Inorg. Chem. 1992, 38:281-322.
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 281-322
    • Cammack, R.1
  • 3
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., Johnson M.K. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 2005, 74:247-281.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 4
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H., Holm R.H., Münck E. Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 1997, 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 6
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 7
    • 38649087966 scopus 로고    scopus 로고
    • Iron-sulfur protein folds, iron-sulfur chemistry, and evolution
    • Meyer J. Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. J. Biol. Inorg. Chem. 2008, 13:157-170.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 157-170
    • Meyer, J.1
  • 8
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: iron-sulfur metalloclusters
    • Rees D.C., Howard J.B. The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science 2003, 300:929-931.
    • (2003) Science , vol.300 , pp. 929-931
    • Rees, D.C.1    Howard, J.B.2
  • 9
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
    • Rouault T.A. Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 2012, 5:155-164.
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 10
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley P.J., Beinert H. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 2003, 6:181-185.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 11
    • 84870323168 scopus 로고    scopus 로고
    • Structure, function and evolution of the XPD family of iron-sulfur-containing 5'->3' DNA helicases
    • White M.F. Structure, function and evolution of the XPD family of iron-sulfur-containing 5'->3' DNA helicases. Biochem. Soc. Trans. 2009, 37:547-551.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 547-551
    • White, M.F.1
  • 12
    • 0018064716 scopus 로고
    • Mössbauer spectroscopy of proteins: Electron carriers
    • Academic Press, F. Sidney, P. Lester (Eds.)
    • Münck E. Mössbauer spectroscopy of proteins: Electron carriers. Methods enzymol 1978, 346-379. Academic Press. F. Sidney, P. Lester (Eds.).
    • (1978) Methods enzymol , pp. 346-379
    • Münck, E.1
  • 14
    • 84866996636 scopus 로고    scopus 로고
    • RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins
    • Lanz N.D., Grove T.L., Gogonea C.B., Lee K.H., Krebs C., Booker S.J. RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins. Methods Enzymol. 2012, 516:125-152.
    • (2012) Methods Enzymol. , vol.516 , pp. 125-152
    • Lanz, N.D.1    Grove, T.L.2    Gogonea, C.B.3    Lee, K.H.4    Krebs, C.5    Booker, S.J.6
  • 15
    • 0001877970 scopus 로고
    • Iron-containing proteins and related analogs - complementary Mössbauer, EPR, and magnetic susceptibility studies
    • Trautwein A.X., Bill E., Bominaar E.L., Winkler H. Iron-containing proteins and related analogs - complementary Mössbauer, EPR, and magnetic susceptibility studies. Struct. Bond. 1991, 78:1-95.
    • (1991) Struct. Bond. , vol.78 , pp. 1-95
    • Trautwein, A.X.1    Bill, E.2    Bominaar, E.L.3    Winkler, H.4
  • 19
    • 0033910009 scopus 로고    scopus 로고
    • Structure and dynamics of biomolecules studied by Mössbauer spectroscopy
    • Schünemann V., Winkler H. Structure and dynamics of biomolecules studied by Mössbauer spectroscopy. Rep. Prog. Phys. 2000, 63:263-353.
    • (2000) Rep. Prog. Phys. , vol.63 , pp. 263-353
    • Schünemann, V.1    Winkler, H.2
  • 22
  • 24
    • 0029467008 scopus 로고
    • Orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters
    • Noodleman L., Peng C.Y., Case D.A., Mouesca J.M. Orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters. Coord. Chem. Rev. 1995, 144:199-244.
    • (1995) Coord. Chem. Rev. , vol.144 , pp. 199-244
    • Noodleman, L.1    Peng, C.Y.2    Case, D.A.3    Mouesca, J.M.4
  • 27
    • 35348849676 scopus 로고    scopus 로고
    • YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase
    • Wu C.H., Jiang W., Krebs C., Stubbe J.A. YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase. Biochemistry 2007, 46:11577-11588.
    • (2007) Biochemistry , vol.46 , pp. 11577-11588
    • Wu, C.H.1    Jiang, W.2    Krebs, C.3    Stubbe, J.A.4
  • 29
    • 11944257212 scopus 로고
    • Interplay of electron exchange and electron-transfer in metal polynuclear complexes in proteins or chemical-models
    • Blondin G., Girerd J.J. Interplay of electron exchange and electron-transfer in metal polynuclear complexes in proteins or chemical-models. Chem. Rev. 1990, 90:1359-1376.
    • (1990) Chem. Rev. , vol.90 , pp. 1359-1376
    • Blondin, G.1    Girerd, J.J.2
  • 30
    • 36749113960 scopus 로고
    • Electron-transfer between magnetic ions in mixed-valence binuclear systems
    • Girerd J.J. Electron-transfer between magnetic ions in mixed-valence binuclear systems. J. Chem. Phys. 1983, 79:1766-1775.
    • (1983) J. Chem. Phys. , vol.79 , pp. 1766-1775
    • Girerd, J.J.1
  • 32
    • 84894226244 scopus 로고    scopus 로고
    • Iron-sulfur bond covalency from electronic structure calculations for classical iron-sulfur clusters
    • Harris T.V., Szilagyi R.K. Iron-sulfur bond covalency from electronic structure calculations for classical iron-sulfur clusters. J. Comput. Chem. 2014, 35:540-552.
    • (2014) J. Comput. Chem. , vol.35 , pp. 540-552
    • Harris, T.V.1    Szilagyi, R.K.2
  • 33
    • 0000384069 scopus 로고
    • Spin-densities and spin coupling in iron-sulfur clusters - a New analysis of hyperfine coupling-constants
    • Mouesca J.M., Noodleman L., Case D.A., Lamotte B. Spin-densities and spin coupling in iron-sulfur clusters - a New analysis of hyperfine coupling-constants. Inorg. Chem. 1995, 34:4347-4359.
    • (1995) Inorg. Chem. , vol.34 , pp. 4347-4359
    • Mouesca, J.M.1    Noodleman, L.2    Case, D.A.3    Lamotte, B.4
  • 34
    • 0015944213 scopus 로고
    • Mössbauer effect in high-potential iron-sulfur protein from Chromatium - evidence for state of iron atoms
    • Dickson D.P.E., Johnson C.E., Cammack R., Evans M.C.W., Hall D.O., Rao K.K. Mössbauer effect in high-potential iron-sulfur protein from Chromatium - evidence for state of iron atoms. Biochem. J. 1974, 139:105-108.
    • (1974) Biochem. J. , vol.139 , pp. 105-108
    • Dickson, D.P.E.1    Johnson, C.E.2    Cammack, R.3    Evans, M.C.W.4    Hall, D.O.5    Rao, K.K.6
  • 35
    • 0017902720 scopus 로고
    • Interpretation of Mössbauer-spectra of 4-iron ferredoxin from Bacillus stearothermophilus
    • Middleton P., Dickson D.P.E., Johnson C.E., Rush J.D. Interpretation of Mössbauer-spectra of 4-iron ferredoxin from Bacillus stearothermophilus. Eur. J. Biochem. 1978, 88:135-141.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 135-141
    • Middleton, P.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4
  • 36
    • 0016249116 scopus 로고
    • Spectroscopic studies on two-iron ferredoxins
    • Sands R.H., Dunham W.R. Spectroscopic studies on two-iron ferredoxins. Q. Rev. Biophys. 1974, 7:443-504.
    • (1974) Q. Rev. Biophys. , vol.7 , pp. 443-504
    • Sands, R.H.1    Dunham, W.R.2
  • 37
    • 0021759095 scopus 로고
    • Purification and characterization of the rieske iron-sulfur protein from Thermus thermophilus - evidence for a [2Fe-2S] cluster having Non-cysteine ligands
    • Fee J.A., Findling K.L., Yoshida T., Hille R., Tarr G.E., Hearshen D.O., Dunham W.R., Day E.P., Kent T.A., Münck E. Purification and characterization of the rieske iron-sulfur protein from Thermus thermophilus - evidence for a [2Fe-2S] cluster having Non-cysteine ligands. J. Biol. Chem. 1984, 259:124-133.
    • (1984) J. Biol. Chem. , vol.259 , pp. 124-133
    • Fee, J.A.1    Findling, K.L.2    Yoshida, T.3    Hille, R.4    Tarr, G.E.5    Hearshen, D.O.6    Dunham, W.R.7    Day, E.P.8    Kent, T.A.9    Münck, E.10
  • 38
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch F., Nicolet Y., Wan J.T., Jarrett J.T., Drennan C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 2004, 303:76-79.
    • (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
  • 40
    • 0034524687 scopus 로고    scopus 로고
    • Ligand K-edge X-ray absorption spectroscopy: A direct probe of ligand-metal covalency
    • Glaser T., Hedman B., Hodgson K.O., Solomon E.I. Ligand K-edge X-ray absorption spectroscopy: A direct probe of ligand-metal covalency. Acc. Chem. Res. 2000, 33:859-868.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 859-868
    • Glaser, T.1    Hedman, B.2    Hodgson, K.O.3    Solomon, E.I.4
  • 43
    • 0019087876 scopus 로고
    • Iron-sulfur proteins - spin-coupling model for 3-iron clusters
    • Kent T.A., Huynh B.H., Münck E. Iron-sulfur proteins - spin-coupling model for 3-iron clusters. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:6574-6576.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6574-6576
    • Kent, T.A.1    Huynh, B.H.2    Münck, E.3
  • 44
    • 0034694686 scopus 로고    scopus 로고
    • Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism
    • Krebs C., Henshaw T.F., Cheek J., Huynh B.H., Broderick J.B. Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism. J. Am. Chem. Soc. 2000, 122:12497-12506.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12497-12506
    • Krebs, C.1    Henshaw, T.F.2    Cheek, J.3    Huynh, B.H.4    Broderick, J.B.5
  • 46
    • 7744224738 scopus 로고
    • Structure and magnetism of iron-sulfur clusters in proteins
    • Münck E., Kent T.A. Structure and magnetism of iron-sulfur clusters in proteins. Hyperfine Interact. 1986, 27:161-172.
    • (1986) Hyperfine Interact. , vol.27 , pp. 161-172
    • Münck, E.1    Kent, T.A.2
  • 47
    • 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., Münck E. Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase. J. Biol. Chem. 1984, 259:4463-4471.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4463-4471
    • Kennedy, M.C.1    Kent, T.A.2    Emptage, M.3    Merkle, H.4    Beinert, H.5    Münck, E.6
  • 48
    • 0036937481 scopus 로고    scopus 로고
    • Formation of a linear 3Fe-4S cluster in a seven-iron ferredoxin triggered by polypeptide unfolding
    • Jones K., Gomes C.M., Huber H., Teixeira M., Wittung-Stafshede P. Formation of a linear 3Fe-4S cluster in a seven-iron ferredoxin triggered by polypeptide unfolding. J. Biol. Inorg. Chem. 2002, 7:357-362.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 357-362
    • Jones, K.1    Gomes, C.M.2    Huber, H.3    Teixeira, M.4    Wittung-Stafshede, P.5
  • 50
    • 84859574521 scopus 로고    scopus 로고
    • Iron-sulfur clusters-new features in enzymes and synthetic models
    • Bill E. Iron-sulfur clusters-new features in enzymes and synthetic models. Hyperfine Interact. 2012, 205:139-147.
    • (2012) Hyperfine Interact. , vol.205 , pp. 139-147
    • Bill, E.1
  • 51
    • 0018881587 scopus 로고
    • Proteins containing 4Fe-4S clusters - an overview
    • Sweeney W.V., Rabinowitz J.C. Proteins containing 4Fe-4S clusters - an overview. Annu. Rev. Biochem. 1980, 49:139-161.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 139-161
    • Sweeney, W.V.1    Rabinowitz, J.C.2
  • 52
    • 0040222479 scopus 로고    scopus 로고
    • Tuning of electron delocalization in polynuclear mixed-valence clusters by super-exchange and double exchange
    • Kröckel M., Grodzicki M., Papaefthymiou V., Trautwein A.X., Kostikas A. Tuning of electron delocalization in polynuclear mixed-valence clusters by super-exchange and double exchange. J. Biol. Inorg. Chem. 1996, 1:173-176.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 173-176
    • Kröckel, M.1    Grodzicki, M.2    Papaefthymiou, V.3    Trautwein, A.X.4    Kostikas, A.5
  • 54
    • 4244192318 scopus 로고
    • Rubredoxin, a simple iron-sulfur protein: its spin hamiltoman and hyperfine parameters
    • (C6-153-C156-158)
    • Schulz C., Debrunner P.G. Rubredoxin, a simple iron-sulfur protein: its spin hamiltoman and hyperfine parameters. J. Phys. Colloq. 1976, 37. (C6-153-C156-158).
    • (1976) J. Phys. Colloq. , vol.37
    • Schulz, C.1    Debrunner, P.G.2
  • 57
    • 0018977856 scopus 로고
    • Interpretation of the Mössbauer-spectra of the high-potential iron protein from Chromatium
    • Middleton P., Dickson D.P.E., Johnson C.E., Rush J.D. Interpretation of the Mössbauer-spectra of the high-potential iron protein from Chromatium. Eur. J. Biochem. 1980, 104:289-296.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 289-296
    • Middleton, P.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4
  • 58
    • 43249088230 scopus 로고    scopus 로고
    • 0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • 0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. J. Biol. Inorg. Chem. 2008, 13:563-574.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 563-574
    • Hans, M.1    Buckel, W.2    Bill, E.3
  • 59
    • 0020807941 scopus 로고
    • Mössbauer and electron paramagnetic resonance studies of activated aconitase - development of a localized valence state at a subsite of the 4Fe-4S cluster on binding of citrate
    • Emptage M.H., Kent T.A., Kennedy M.C., Beinert H., Münck E. Mössbauer and electron paramagnetic resonance studies of activated aconitase - development of a localized valence state at a subsite of the 4Fe-4S cluster on binding of citrate. Proc. Natl. Acad. Sci. U. S. A. 1983, 80:4674-4678.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 4674-4678
    • Emptage, M.H.1    Kent, T.A.2    Kennedy, M.C.3    Beinert, H.4    Münck, E.5
  • 60
    • 0037065661 scopus 로고    scopus 로고
    • Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: A Mössbauer spectroscopic study
    • Krebs C., Broderick W.E., Henshaw T.F., Broderick J.B., Huynh B.H. Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: A Mössbauer spectroscopic study. J. Am. Chem. Soc. 2002, 124:912-913.
    • (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
  • 67
    • 0034712709 scopus 로고    scopus 로고
    • Unusual spectroscopic and electrochemical properties of the 2[4Fe-4S] ferredoxin of Thauera aromatica
    • Boll M., Fuchs G., Tilley G., Armstrong F.A., Lowe D.J. Unusual spectroscopic and electrochemical properties of the 2[4Fe-4S] ferredoxin of Thauera aromatica. Biochemistry 2000, 39:4929-4938.
    • (2000) Biochemistry , vol.39 , pp. 4929-4938
    • Boll, M.1    Fuchs, G.2    Tilley, G.3    Armstrong, F.A.4    Lowe, D.J.5
  • 69
    • 0019767395 scopus 로고
    • Replacement of sulfide by selenide in the [4Fe-4S] clusters of the ferredoxin from Clostridium pasteurianum
    • Meyer J., Moulis J.M. Replacement of sulfide by selenide in the [4Fe-4S] clusters of the ferredoxin from Clostridium pasteurianum. Biochem. Biophys. Res. Commun. 1981, 103:667-673.
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 667-673
    • Meyer, J.1    Moulis, J.M.2
  • 70
    • 0032263876 scopus 로고    scopus 로고
    • Iron-sulfur clusters and their electronic and magnetic properties
    • Mouesca J.M., Lamotte B. Iron-sulfur clusters and their electronic and magnetic properties. Coord. Chem. Rev. 1998, 178:1573-1614.
    • (1998) Coord. Chem. Rev. , vol.178 , pp. 1573-1614
    • Mouesca, J.M.1    Lamotte, B.2
  • 73
    • 14644443590 scopus 로고    scopus 로고
    • Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus
    • Guiral M., Aubert T., Giudici-Orticoni M.T. Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus. Biochem. Soc. Trans. 2005, 33:22-24.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 22-24
    • Guiral, M.1    Aubert, T.2    Giudici-Orticoni, M.T.3
  • 77
    • 79955027963 scopus 로고    scopus 로고
    • Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus
    • Pandelia M.E., Nitschke W., Infossi P., Giudici-Orticoni M.T., Bill E., Lubitz W. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:6097-6102.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6097-6102
    • Pandelia, M.E.1    Nitschke, W.2    Infossi, P.3    Giudici-Orticoni, M.T.4    Bill, E.5    Lubitz, W.6
  • 78
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Shomura Y., Yoon K.S., Nishihara H., Higuchi Y. Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 2011, 479:253-256.
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 81
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods
    • Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 2001, 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
  • 82
    • 65249142024 scopus 로고    scopus 로고
    • Anaerobic functionalization of unactivated C-H bonds
    • Booker S.J. Anaerobic functionalization of unactivated C-H bonds. Curr. Opin. Chem. Biol. 2009, 13:58-73.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 58-73
    • Booker, S.J.1
  • 84
    • 84927166656 scopus 로고    scopus 로고
    • The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor
    • De Gruyter, Berlin, T.A. Rouault (Ed.)
    • Lanz N.D., Booker S.J. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor. Iron-sulfur clusters in chemistry and biology 2014, De Gruyter, Berlin. T.A. Rouault (Ed.).
    • (2014) Iron-sulfur clusters in chemistry and biology
    • Lanz, N.D.1    Booker, S.J.2
  • 85
    • 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 R.M., Booker S.J. 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, 127:2860-2861.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 88
    • 84866036753 scopus 로고    scopus 로고
    • Biotin synthase: insights into radical-mediated carbon-sulfur bond formation
    • Fugate C.J., Jarrett J.T. Biotin synthase: insights into radical-mediated carbon-sulfur bond formation. Biochim. Biophys. Acta 2012, 1824:1213-1222.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1213-1222
    • Fugate, C.J.1    Jarrett, J.T.2
  • 90
    • 80052738180 scopus 로고    scopus 로고
    • Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase
    • Taylor A.M., Stoll S., Britt R.D., Jarrett J.T. Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase. Biochemistry 2011, 50:7953-7963.
    • (2011) Biochemistry , vol.50 , pp. 7953-7963
    • Taylor, A.M.1    Stoll, S.2    Britt, R.D.3    Jarrett, J.T.4
  • 92
    • 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 P.L. Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner. Angew. Chem. Int. Ed. 2006, 45:5197-5199.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 5197-5199
    • Douglas, P.1    Kriek, M.2    Bryant, P.3    Roach, P.L.4
  • 93
    • 84904628766 scopus 로고    scopus 로고
    • Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase
    • Lanz N.D., Pandelia M.E., Kakar E.S., Lee K.H., Krebs C., Booker S.J. Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase. Biochemistry 2014, 53:4557-4572.
    • (2014) Biochemistry , vol.53 , pp. 4557-4572
    • Lanz, N.D.1    Pandelia, M.E.2    Kakar, E.S.3    Lee, K.H.4    Krebs, C.5    Booker, S.J.6
  • 94
    • 0032505869 scopus 로고    scopus 로고
    • Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli
    • Popescu C.V., Bates D.M., Beinert H., Münck E., Kiley P.J. Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:13431-13435.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 13431-13435
    • Popescu, C.V.1    Bates, D.M.2    Beinert, H.3    Münck, E.4    Kiley, P.J.5
  • 99
  • 100
    • 84896881843 scopus 로고    scopus 로고
    • Glycyl radical activating enzymes: structure, mechanism, and substrate interactions
    • Shisler K.A., Broderick J.B. Glycyl radical activating enzymes: structure, mechanism, and substrate interactions. Arch. Biochem. Biophys. 2014, 546:64-71.
    • (2014) Arch. Biochem. Biophys. , vol.546 , pp. 64-71
    • Shisler, K.A.1    Broderick, J.B.2
  • 103
    • 77954202742 scopus 로고    scopus 로고
    • Biophysical characterization of iron in mitochondria isolated from respiring and fermenting yeast
    • Morales J.G., Holmes-Hampton G.P., Miao R., Guo Y.S., Münck E., Lindahl P.A. Biophysical characterization of iron in mitochondria isolated from respiring and fermenting yeast. Biochemistry 2010, 49:5436-5444.
    • (2010) Biochemistry , vol.49 , pp. 5436-5444
    • Morales, J.G.1    Holmes-Hampton, G.P.2    Miao, R.3    Guo, Y.S.4    Münck, E.5    Lindahl, P.A.6


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