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Volumn 52, Issue 48, 2013, Pages 8696-8707

Biochemical and kinetic characterization of radical S -Adenosyl- L -Methionine enzyme HydG

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM ACETOBUTYLICUM; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; IRON-SULFUR CLUSTERS; KINETIC CHARACTERIZATION; MICHAELIS-MENTEN CONSTANT; S ADENOSYL L METHIONINES; SPECTROSCOPIC COMPARISON; UV VISIBLE SPECTROSCOPY;

EID: 84889262342     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401143s     Document Type: Article
Times cited : (44)

References (75)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • DOI 10.1021/cr050196r
    • Vignais, P. M. and Billoud, B. (2007) Occurrence, Classification, and Biological Function of Hydrogenases: An Overview Chem. Rev. 107, 4206-4272 (Pubitemid 350041744)
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 3
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters, J. W., Lanzilotta, W. N., Lemon, B. J., and Seefeldt, L. C. (1998) X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution Science 282, 1853-1858 (Pubitemid 28555258)
    • (1998) Science , vol.282 , Issue.5395 , pp. 1853-1858
    • Peters, J.W.1
  • 4
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • DOI 10.1016/S0969-2126(99)80005-7
    • Nicolet, Y., Piras, C., Legrand, P., Hatchikian, C. E., and Fontecilla-Camps, J. C. (1999) Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center Structure 7, 13-23 (Pubitemid 29159178)
    • (1999) Structure , vol.7 , Issue.1 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 5
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • DOI 10.1021/ja0020963
    • Nicolet, Y., de Lacey, A. L., Vernède, X., Fernandez, V. M., Hatchikian, E. C., and Fontecilla-Camps, J. C. (2001) Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibrio desulfuricans J. Am. Chem. Soc. 123, 1596-1601 (Pubitemid 32179408)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.8 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2    Vernede, X.3    Fernandez, V.M.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 6
    • 77950818400 scopus 로고    scopus 로고
    • Quantum Refinement of [FeFe] Hydrogenase Indicates a Dithiomethylamine Ligand
    • Ryde, U., Greco, C., and De Gioia, L. (2010) Quantum Refinement of [FeFe] Hydrogenase Indicates a Dithiomethylamine Ligand J. Am. Chem. Soc. 132, 4512-4513
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4512-4513
    • Ryde, U.1    Greco, C.2    De Gioia, L.3
  • 7
    • 68349101212 scopus 로고    scopus 로고
    • 14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: Evidence for a nitrogen in the dithiol bridge
    • 14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: Evidence for a nitrogen in the dithiol bridge Phys. Chem. Chem. Phys. 11, 6592-6599
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6592-6599
    • Silakov, A.1    Wenk, B.2    Reijerse, E.3    Lubitz, W.4
  • 13
    • 50249150760 scopus 로고    scopus 로고
    • Desulfovibrio vulgaris Hildenborough HydE and HydG interact with the HydA subunit of the [FeFe] hydrogenase
    • Mansure, J. J. and Hallenbeck, P. C. (2008) Desulfovibrio vulgaris Hildenborough HydE and HydG interact with the HydA subunit of the [FeFe] hydrogenase Biotechnol. Lett. 30, 1765-1769
    • (2008) Biotechnol. Lett. , vol.30 , pp. 1765-1769
    • Mansure, J.J.1    Hallenbeck, P.C.2
  • 14
    • 84866658489 scopus 로고    scopus 로고
    • New Insights into [FeFe] Hydrogenase Activation and Maturase Function
    • Kuchenreuther, J. M., Britt, R. D., and Swartz, J. R. (2012) New Insights into [FeFe] Hydrogenase Activation and Maturase Function PLoS One 7, e45850
    • (2012) PLoS One , vol.7 , pp. 45850
    • Kuchenreuther, J.M.1    Britt, R.D.2    Swartz, J.R.3
  • 15
    • 58949084423 scopus 로고    scopus 로고
    • The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly
    • Pilet, E., Nicolet, Y., Mathevon, C., Douki, T., Fontecilla-Camps, J. C., and Fontecave, M. (2009) The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly FEBS Lett. 583, 506-511
    • (2009) FEBS Lett. , vol.583 , pp. 506-511
    • Pilet, E.1    Nicolet, Y.2    Mathevon, C.3    Douki, T.4    Fontecilla-Camps, J.C.5    Fontecave, M.6
  • 20
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • DOI 10.1016/j.febslet.2005.07.092, PII S0014579305009889
    • Rubach, J. K., Brazzolotto, X., Gaillard, J., and Fontecave, M. (2005) Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima FEBS Lett. 579, 5055-5060 (Pubitemid 41242852)
    • (2005) FEBS Letters , vol.579 , Issue.22 , pp. 5055-5060
    • Rubach, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 21
    • 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., and Miller, N. E. (2001) 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. 29, 1097-1106 (Pubitemid 32186195)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 23
    • 0037174377 scopus 로고    scopus 로고
    • An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S -Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme
    • Walsby, C., Ortillo, D., Broderick, W. E., Broderick, J. B., and Hoffman, B. M. (2002) An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S -Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme J. Am. Chem. Soc. 124, 11270-11271
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 24
    • 79954499453 scopus 로고    scopus 로고
    • Structural Insights into Radical Generation by the Radical SAM Superfamily
    • Vey, J. L. and Drennan, C. L. (2011) Structural Insights into Radical Generation by the Radical SAM Superfamily Chem. Rev. 111, 2487-2506
    • (2011) Chem. Rev. , vol.111 , pp. 2487-2506
    • Vey, J.L.1    Drennan, C.L.2
  • 25
    • 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
    • DOI 10.1021/ja017562i
    • Krebs, C., Broderick, W. E., Henshaw, T. F., Broderick, J. B., and Huynh, B. H. (2002) 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. 124, 912-913 (Pubitemid 34130969)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.6 , pp. 912-913
    • Krebs, C.1    Broderick, W.E.2    Henshaw, T.F.3    Broderick, J.B.4    Huynh, B.H.5
  • 27
  • 28
    • 0034734328 scopus 로고    scopus 로고
    • 1+ Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover
    • 1+ Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover 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
  • 29
    • 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 [22]
    • DOI 10.1021/ja9925507
    • Magnusson, O. T., Reed, G. H., and Frey, P. A. (1999) 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. 121, 9764-9765 (Pubitemid 29498517)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.41 , pp. 9764-9765
    • Magnusson, O.Th.1    Reed, G.H.2    Frey, P.A.3
  • 32
    • 37349127348 scopus 로고    scopus 로고
    • Thiamine biosynthesis in Escherichia coli: Identification of the intermediate and by-product derived from tyrosine
    • DOI 10.1002/anie.200702554
    • Kriek, M., Martins, F., Challand, M. R., Croft, A., and Roach, P. L. (2007) Thiamine Biosynthesis in Escherichia coli: Identification of the Intermediate and By-Product Derived from Tyrosine Angew. Chem., Int. Ed. 46, 9223-9226 (Pubitemid 350292146)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.48 , pp. 9223-9226
    • Kriek, M.1    Martins, F.2    Challand, M.R.3    Croft, A.4    Roach, P.L.5
  • 33
    • 77949318133 scopus 로고    scopus 로고
    • Catalytic Activity of the Anaerobic Tyrosine Lyase Required for Thiamine Biosynthesis in Escherichia coli
    • Challand, M. R., Martins, F. T., and Roach, P. L. (2010) Catalytic Activity of the Anaerobic Tyrosine Lyase Required for Thiamine Biosynthesis in Escherichia coli J. Biol. Chem. 285, 5240-5248
    • (2010) J. Biol. Chem. , vol.285 , pp. 5240-5248
    • Challand, M.R.1    Martins, F.T.2    Roach, P.L.3
  • 34
    • 79951845926 scopus 로고    scopus 로고
    • Radical-mediated enzymatic carbon chain fragmentation-recombination
    • Zhang, Q., Li, Y., Chen, D., Yu, Y., Duan, L., Shen, B., and Liu, W. (2011) Radical-mediated enzymatic carbon chain fragmentation-recombination Nat. Chem. Biol. 7, 154-160
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 154-160
    • Zhang, Q.1    Li, Y.2    Chen, D.3    Yu, Y.4    Duan, L.5    Shen, B.6    Liu, W.7
  • 35
    • 70350170631 scopus 로고    scopus 로고
    • Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework
    • Yu, Y., Duan, L., Zhang, Q., Liao, R., Ding, Y., Pan, H., Wendt-Pienkowski, E., Tang, G., Shen, B., and Liu, W. (2009) Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework ACS Chem. Biol. 4, 855-864
    • (2009) ACS Chem. Biol. , vol.4 , pp. 855-864
    • Yu, Y.1    Duan, L.2    Zhang, Q.3    Liao, R.4    Ding, Y.5    Pan, H.6    Wendt-Pienkowski, E.7    Tang, G.8    Shen, B.9    Liu, W.10
  • 36
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • DOI 10.1128/JB.188.6.2163-2172.2006
    • King, P. W., Posewitz, M. C., Ghirardi, M. L., and Seibert, M. (2006) Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System J. Bacteriol. 188, 2163-2172 (Pubitemid 43376470)
    • (2006) Journal of Bacteriology , vol.188 , Issue.6 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 38
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • Lanz, N. D. and Booker, S. J. (2012) Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes Biochim. Biophys. Acta 1824, 1196-1212
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2
  • 39
    • 77957134413 scopus 로고    scopus 로고
    • A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG
    • Nicolet, Y., Martin, L., Tron, C., and Fontecilla-Camps, J. C. (2010) A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG FEBS Lett. 584, 4197-4202
    • (2010) FEBS Lett. , vol.584 , pp. 4197-4202
    • Nicolet, Y.1    Martin, L.2    Tron, C.3    Fontecilla-Camps, J.C.4
  • 41
    • 84879811872 scopus 로고    scopus 로고
    • Cysteine Methylation Controls Radical Generation in the Cfr Radical AdoMet rRNA Methyltransferase
    • Challand, M. R., Salvadori, E., Driesener, R. C., Kay, C. W. M., Roach, P. L., and Spencer, J. (2013) Cysteine Methylation Controls Radical Generation in the Cfr Radical AdoMet rRNA Methyltransferase PLoS One 8, e67979
    • (2013) PLoS One , vol.8 , pp. 67979
    • Challand, M.R.1    Salvadori, E.2    Driesener, R.C.3    Kay, C.W.M.4    Roach, P.L.5    Spencer, J.6
  • 42
    • 78649312971 scopus 로고    scopus 로고
    • Biotin Synthase Exhibits Burst Kinetics and Multiple Turnovers in the Absence of Inhibition by Products and Product-Related Biomolecules
    • Farrar, C. E., Siu, K. K. W., Howell, P. L., and Jarrett, J. T. (2010) Biotin Synthase Exhibits Burst Kinetics and Multiple Turnovers in the Absence of Inhibition by Products and Product-Related Biomolecules Biochemistry 49, 9985-9996
    • (2010) Biochemistry , vol.49 , pp. 9985-9996
    • Farrar, C.E.1    Siu, K.K.W.2    Howell, P.L.3    Jarrett, J.T.4
  • 43
    • 0031561804 scopus 로고    scopus 로고
    • Differential binding of S-adenosylmethionine S-adenosylhomocysteine and sinefungin to the adenine-specific DNA methyltransferase M. TaqI
    • DOI 10.1006/jmbi.1996.0711
    • Schluckebier, G., Kozak, M., Bleimling, N., Weinhold, E., and Saenger, W. (1997) Differential binding of S -adenosylmethionine, S -adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI J. Mol. Biol. 265, 56-67 (Pubitemid 27110565)
    • (1997) Journal of Molecular Biology , vol.265 , Issue.1 , pp. 56-67
    • Schluckebier, G.1    Kozak, M.2    Bleimling, N.3    Weinhold, E.4    Saenger, W.5
  • 44
    • 0013905989 scopus 로고
    • Methods for the analysis and preparation of adenosylmethionine and adenosylhomocysteine
    • Shapiro, S. K. and Ehninger, D. J. (1966) Methods for the analysis and preparation of adenosylmethionine and adenosylhomocysteine Anal. Biochem. 15, 323-333
    • (1966) Anal. Biochem. , vol.15 , pp. 323-333
    • Shapiro, S.K.1    Ehninger, D.J.2
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish, W. W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples Methods Enzymol. 158, 357-364
    • (1988) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 47
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • DOI 10.1016/j.jmr.2005.08.013, PII S1090780705002892
    • Stoll, S. and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178, 42-55 (Pubitemid 41774010)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.1 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 48
    • 0033524910 scopus 로고    scopus 로고
    • Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases
    • Pierik, A. J., Roseboom, W., Happe, R. P., Bagley, K. A., and Albracht, S. P. J. (1999) Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases J. Biol. Chem. 274, 3331-3337
    • (1999) J. Biol. Chem. , vol.274 , pp. 3331-3337
    • Pierik, A.J.1    Roseboom, W.2    Happe, R.P.3    Bagley, K.A.4    Albracht, S.P.J.5
  • 49
  • 50
    • 80053394442 scopus 로고    scopus 로고
    • The Original Michaelis Constant: Translation of the 1913 Michaelis-Menten Paper
    • Johnson, K. A. and Goody, R. S. (2011) The Original Michaelis Constant: Translation of the 1913 Michaelis-Menten Paper Biochemistry 50, 8264-8269
    • (2011) Biochemistry , vol.50 , pp. 8264-8269
    • Johnson, K.A.1    Goody, R.S.2
  • 51
    • 0018881587 scopus 로고
    • Proteins Containing 4Fe-4S Clusters: An Overview
    • Sweeney, W. V. and Rabinowitz, J. C. (1980) Proteins Containing 4Fe-4S Clusters: An Overview Annu. Rev. Biochem. 49, 139-161
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 139-161
    • Sweeney, W.V.1    Rabinowitz, J.C.2
  • 52
    • 33644860151 scopus 로고    scopus 로고
    • 2+/1+ in lysine 2,3-aminomutase
    • DOI 10.1021/bi0519497
    • 2+/1+ in Lysine 2,3-Aminomutase Biochemistry 45, 3219-3225 (Pubitemid 43376340)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3219-3225
    • Hinckley, G.T.1    Frey, P.A.2
  • 53
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5′-GTP to the C-terminal FeS cluster of the radical S -adenosylmethionine enzyme MoaA provides insights into its mechanism
    • Hänzelmann, P. and Schindelin, H. (2006) Binding of 5′-GTP to the C-terminal FeS cluster of the radical S -adenosylmethionine enzyme MoaA provides insights into its mechanism Proc. Natl. Acad. Sci. U.S.A. 103, 6829-6834
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6829-6834
    • Hänzelmann, P.1    Schindelin, H.2
  • 54
    • 67649976798 scopus 로고    scopus 로고
    • ENDOR Spectroscopy Shows That Guanine N1 Binds to [4Fe-4S] Cluster II of the S -Adenosylmethionine-Dependent Enzyme MoaA: Mechanistic Implications
    • Lees, N. S., Hänzelmann, P., Hernandez, H. L., Subramanian, S., Schindelin, H., Johnson, M. K., and Hoffman, B. M. (2009) ENDOR Spectroscopy Shows That Guanine N1 Binds to [4Fe-4S] Cluster II of the S -Adenosylmethionine- Dependent Enzyme MoaA: Mechanistic Implications J. Am. Chem. Soc. 131, 9184-9185
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9184-9185
    • Lees, N.S.1    Hänzelmann, P.2    Hernandez, H.L.3    Subramanian, S.4    Schindelin, H.5    Johnson, M.K.6    Hoffman, B.M.7
  • 57
    • 0037192119 scopus 로고    scopus 로고
    • Crystal structure and stability studies of C77S HiPIP: A serine ligated [4Fe-4S] cluster
    • DOI 10.1021/bi011811y
    • Mansy, S. S., Xiong, Y., Hemann, C., Hille, R., Sundaralingam, M., and Cowan, J. A. (2002) Crystal Structure and Stability Studies of C77S HiPIP: A Serine Ligated [4Fe-4S] Cluster Biochemistry 41, 1195-1201 (Pubitemid 34086920)
    • (2002) Biochemistry , vol.41 , Issue.4 , pp. 1195-1201
    • Mansy, S.S.1    Xiong, Y.2    Hemann, C.3    Hille, R.4    Sundaralingam, M.5    Cowan, J.A.6
  • 58
    • 0032490087 scopus 로고    scopus 로고
    • The rubredoxin from Clostridium pasteurianum: Mutation of the iron cysteinyl ligands to serine. Crystal and molecular structures of oxidized and dithionite-treated forms of the Cys42Ser mutant
    • DOI 10.1021/ja973162c
    • Xiao, Z., Lavery, M. J., Ayhan, M., Scrofani, S. D. B., Wilce, M. C. J., Guss, J. M., Tregloan, P. A., George, G. N., and Wedd, A. G. (1998) The Rubredoxin from Clostridium pasteurianum: Mutation of the Iron Cysteinyl Ligands to Serine. Crystal and Molecular Structures of Oxidized and Dithionite-Treated Forms of the Cys42Ser Mutant J. Am. Chem. Soc. 120, 4135-4150 (Pubitemid 28248336)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.17 , pp. 4135-4150
    • Xiao, Z.1    Lavery, M.J.2    Ayhan, M.3    Scrofani, S.D.B.4    Wilce, M.C.J.5    Guss, J.M.6    Tregloan, P.A.7    George, G.N.8    Wedd, A.G.9
  • 60
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • Dailey, H. A., Finnegan, M. G., and Johnson, M. K. (1994) Human ferrochelatase is an iron-sulfur protein Biochemistry 33, 403-407 (Pubitemid 24048081)
    • (1994) Biochemistry , vol.33 , Issue.2 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 61
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
    • DOI 10.1021/ja072481t
    • Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D., and Eguchi, T. (2007) Characterization and Mechanistic Study of a Radical SAM Dehydrogenase in the Biosynthesis of Butirosin J. Am. Chem. Soc. 129, 15147-15155 (Pubitemid 350247798)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.49 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 63
    • 84872108164 scopus 로고    scopus 로고
    • Spectroscopic, Steady-State Kinetic, and Mechanistic Characterization of the Radical SAM Enzyme QueE, Which Catalyzes a Complex Cyclization Reaction in the Biosynthesis of 7-Deazapurines
    • McCarty, R. M., Krebs, C., and Bandarian, V. (2013) Spectroscopic, Steady-State Kinetic, and Mechanistic Characterization of the Radical SAM Enzyme QueE, Which Catalyzes a Complex Cyclization Reaction in the Biosynthesis of 7-Deazapurines Biochemistry 52, 188-198
    • (2013) Biochemistry , vol.52 , pp. 188-198
    • McCarty, R.M.1    Krebs, C.2    Bandarian, V.3
  • 64
    • 83055188821 scopus 로고    scopus 로고
    • Metabolome Remodeling during the Acidogenic-Solventogenic Transition in Clostridium acetobutylicum
    • Amador-Noguez, D., Brasg, I. A., Feng, X.-J., Roquet, N., and Rabinowitz, J. D. (2011) Metabolome Remodeling during the Acidogenic-Solventogenic Transition in Clostridium acetobutylicum Appl. Environ. Microbiol. 77, 7984-7997
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7984-7997
    • Amador-Noguez, D.1    Brasg, I.A.2    Feng, X.-J.3    Roquet, N.4    Rabinowitz, J.D.5
  • 66
    • 0345074385 scopus 로고
    • The solubility of tyrosine in acid and in alkali
    • Hitchcock, D. I. (1924) The solubility of tyrosine in acid and in alkali J. Gen. Physiol. 6, 747-757
    • (1924) J. Gen. Physiol. , vol.6 , pp. 747-757
    • Hitchcock, D.I.1
  • 68
    • 0141620318 scopus 로고    scopus 로고
    • Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase
    • DOI 10.1021/ja036120z
    • 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 (Pubitemid 37175392)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.39 , pp. 11788-11789
    • Chen, D.1    Walsby, C.2    Hoffman, B.M.3    Frey, P.A.4
  • 69
    • 84866021687 scopus 로고    scopus 로고
    • Structural diversity in the AdoMet radical enzyme superfamily
    • Dowling, D. P., Vey, J. L., Croft, A. K., and Drennan, C. L. (2012) Structural diversity in the AdoMet radical enzyme superfamily Biochim. Biophys. Acta 1824, 1178-1195
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1178-1195
    • Dowling, D.P.1    Vey, J.L.2    Croft, A.K.3    Drennan, C.L.4
  • 70
    • 84856367380 scopus 로고    scopus 로고
    • Radical S -adenosylmethionine enzymes: Mechanism, control and function
    • Challand, M. R., Driesener, R. C., and Roach, P. L. (2011) Radical S -adenosylmethionine enzymes: Mechanism, control and function Nat. Prod. Rep. 28, 1696-1721
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1696-1721
    • Challand, M.R.1    Driesener, R.C.2    Roach, P.L.3
  • 71
    • 84878137190 scopus 로고    scopus 로고
    • X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification
    • Goldman, P. J., Grove, T. L., Sites, L. A., McLaughlin, M. I., Booker, S. J., and Drennan, C. L. (2013) X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification Proc. Natl. Acad. Sci. U.S.A. 110, 8519-8524
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8519-8524
    • Goldman, P.J.1    Grove, T.L.2    Sites, L.A.3    McLaughlin, M.I.4    Booker, S.J.5    Drennan, C.L.6
  • 72
    • 84877062815 scopus 로고    scopus 로고
    • Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in the Mechanism of Catalysis
    • Grove, T. L., Ahlum, J. H., Qin, R. M., Lanz, N. D., Radle, M. I., Krebs, C., and Booker, S. J. (2013) Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in the Mechanism of Catalysis Biochemistry 52, 2874-2887
    • (2013) Biochemistry , vol.52 , pp. 2874-2887
    • Grove, T.L.1    Ahlum, J.H.2    Qin, R.M.3    Lanz, N.D.4    Radle, M.I.5    Krebs, C.6    Booker, S.J.7
  • 73
    • 77951930923 scopus 로고    scopus 로고
    • A Consensus Mechanism for Radical SAM-Dependent Dehydrogenation? BtrN Contains Two [4Fe-4S] Clusters
    • Grove, T. L., Ahlum, J. H., Sharma, P., Krebs, C., and Booker, S. J. (2010) A Consensus Mechanism for Radical SAM-Dependent Dehydrogenation? BtrN Contains Two [4Fe-4S] Clusters Biochemistry 49, 3783-3785
    • (2010) Biochemistry , vol.49 , pp. 3783-3785
    • Grove, T.L.1    Ahlum, J.H.2    Sharma, P.3    Krebs, C.4    Booker, S.J.5
  • 74
    • 84885045053 scopus 로고    scopus 로고
    • X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry
    • Goldman, P. J., Grove, T. L., Booker, S. J., and Drennan, C. L. (2013) X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry Proc. Natl. Acad. Sci. U.S.A. 110, 15949-15954
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 15949-15954
    • Goldman, P.J.1    Grove, T.L.2    Booker, S.J.3    Drennan, C.L.4


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