메뉴 건너뛰기




Volumn 1844, Issue 12, 2014, Pages 2135-2144

Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217

Author keywords

Cobalamin; Methyltransferase; Phosphinate; Radical S adenosyl l methionine

Indexed keywords

CITRIC ACID; COBALAMIN; DEMETHYLPHOSPHINOTHRICIN; HYDROXOCOBALAMIN; MECOBALAMIN; METHYLTRANSFERASE; N ACETYL DEMETHYLPHOSPHINOTHRICIN; N ACETYL PHOSPHINOTHRICIN; PHOSPHINOTHRICIN; PHOSPHINOTHRICIN DERIVATIVE; RADICAL S ADENOSYL L METHIONINE METHYLTRANSFERASE PHPK; REDUCING AGENT; TITANIUM CITRATE; UNCLASSIFIED DRUG;

EID: 84907652999     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.09.009     Document Type: Article
Times cited : (26)

References (71)
  • 1
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • W.W. Metcalf, and W.A. van der Donk Biosynthesis of phosphonic and phosphinic acid natural products Annu. Rev. Biochem. 78 2009 65 94
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 2
    • 0018932939 scopus 로고
    • The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl-shikimic acid-3-phosphate synthase
    • H.C. Steinrucken, and N. Amrhein The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl-shikimic acid-3-phosphate synthase Biochem. Biophys. Res. Commun. 94 1980 1207 1212
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1207-1212
    • Steinrucken, H.C.1    Amrhein, N.2
  • 3
    • 27844455955 scopus 로고    scopus 로고
    • Acyclic nucleoside phosphonates: A key class of antiviral drugs
    • E. De Clercq, and A. Holy Acyclic nucleoside phosphonates: a key class of antiviral drugs Nat. Rev. Drug Discov. 4 2005 928 940
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 928-940
    • De Clercq, E.1    Holy, A.2
  • 6
    • 0035916242 scopus 로고    scopus 로고
    • The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition
    • H.S. Gill, and D. Eisenberg The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition Biochemistry 40 2001 1903 1912
    • (2001) Biochemistry , vol.40 , pp. 1903-1912
    • Gill, H.S.1    Eisenberg, D.2
  • 7
    • 0025867099 scopus 로고
    • Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench kinetic technique
    • L.M. Abell, and J.J. Villafranca Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench kinetic technique Biochemistry 30 1991 6135 6141
    • (1991) Biochemistry , vol.30 , pp. 6135-6141
    • Abell, L.M.1    Villafranca, J.J.2
  • 9
    • 0021151918 scopus 로고
    • Phosalacine, a new herbicidal antibiotic containing phosphinothricin. Fermentation, isolation, biological activity and mechanism of action
    • S. Omura, M. Murata, H. Hanaki, K. Hinotozawa, R. Oiwa, and H. Tanaka Phosalacine, a new herbicidal antibiotic containing phosphinothricin. Fermentation, isolation, biological activity and mechanism of action J. Antibiot. (Tokyo) 37 1984 829 835
    • (1984) J. Antibiot. (Tokyo) , vol.37 , pp. 829-835
    • Omura, S.1    Murata, M.2    Hanaki, H.3    Hinotozawa, K.4    Oiwa, R.5    Tanaka, H.6
  • 11
    • 10444251153 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide from Streptomyces viridochromogenes Tü494
    • D. Schwartz, S. Berger, E. Heinzelmann, K. Muschko, K. Welzel, and W. Wohlleben Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide from Streptomyces viridochromogenes Tü494 Appl. Environ. Microbiol. 70 2004 7093 7102
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 7093-7102
    • Schwartz, D.1    Berger, S.2    Heinzelmann, E.3    Muschko, K.4    Welzel, K.5    Wohlleben, W.6
  • 12
    • 11244354656 scopus 로고    scopus 로고
    • Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736
    • J.A. Blodgett, J.K. Zhang, and W.W. Metcalf Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736 Antimicrob. Agents Chemother. 49 2005 230 240
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 230-240
    • Blodgett, J.A.1    Zhang, J.K.2    Metcalf, W.W.3
  • 13
    • 0026724852 scopus 로고
    • Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: Discovery of a P-methylation enzyme
    • K. Kamigiri, T. Hidaka, S. Imai, T. Murakami, and H. Seto Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme J. Antibiot. (Tokyo) 45 1992 781 787
    • (1992) J. Antibiot. (Tokyo) , vol.45 , pp. 781-787
    • Kamigiri, K.1    Hidaka, T.2    Imai, S.3    Murakami, T.4    Seto, H.5
  • 14
    • 0021879482 scopus 로고
    • Studies on the biosynthesis of bialaphos (SF-1293). 6. Production of N-acetyl-demethylphosphinothricin and N-acetylbialaphos by blocked mutants of Streptomyces hygroscopicus SF-1293 and their roles in the biosynthesis of bialaphos
    • S. Imai, H. Seto, T. Sasaki, T. Tsuruoka, H. Ogawa, A. Satoh, S. Inouye, T. Niida, and N. Otake Studies on the biosynthesis of bialaphos (SF-1293). 6. Production of N-acetyl-demethylphosphinothricin and N-acetylbialaphos by blocked mutants of Streptomyces hygroscopicus SF-1293 and their roles in the biosynthesis of bialaphos J. Antibiot. (Tokyo) 38 1985 687 690
    • (1985) J. Antibiot. (Tokyo) , vol.38 , pp. 687-690
    • Imai, S.1    Seto, H.2    Sasaki, T.3    Tsuruoka, T.4    Ogawa, H.5    Satoh, A.6    Inouye, S.7    Niida, T.8    Otake, N.9
  • 15
    • 80055010853 scopus 로고    scopus 로고
    • In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea
    • W.J. Werner, K.D. Allen, K. Hu, G.L. Helms, B.S. Chen, and S.C. Wang In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea Biochemistry 50 2011 8986 8988
    • (2011) Biochemistry , vol.50 , pp. 8986-8988
    • Werner, W.J.1    Allen, K.D.2    Hu, K.3    Helms, G.L.4    Chen, B.S.5    Wang, S.C.6
  • 16
    • 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
    • H.J. Sofia, G. Chen, B.G. Hetzler, J.F. Reyes-Spindola, and N.E. Miller 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 2001 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
  • 18
    • 84859891708 scopus 로고    scopus 로고
    • Radical-mediated enzymatic methylation: A tale of two SAMs
    • Q. Zhang, W.A. van der Donk, and W. Liu Radical-mediated enzymatic methylation: a tale of two SAMs Acc. Chem. Res. 45 2011 555 564
    • (2011) Acc. Chem. Res. , vol.45 , pp. 555-564
    • Zhang, Q.1    Van Der Donk, W.A.2    Liu, W.3
  • 20
    • 84878651511 scopus 로고    scopus 로고
    • The GenK-catalyzed C-6′ methylation in the biosynthesis of gentamicin: Isolation and characterization of a cobalamin-dependent radical SAM enzyme
    • H.J. Kim, R.M. McCarty, Y. Ogasawara, Y.N. Liu, S.O. Mansoorabadi, J. Levieux, and H.W. Liu The GenK-catalyzed C-6′ methylation in the biosynthesis of gentamicin: isolation and characterization of a cobalamin-dependent radical SAM enzyme J. Am. Chem. Soc. 135 2013 8093 8096
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8093-8096
    • Kim, H.J.1    McCarty, R.M.2    Ogasawara, Y.3    Liu, Y.N.4    Mansoorabadi, S.O.5    Levieux, J.6    Liu, H.W.7
  • 21
    • 84892772585 scopus 로고    scopus 로고
    • Initial characterization of Fom3 from Streptomyces wedmorensis, the methyltransferase in fosfomycin biosynthesis
    • K.D. Allen, and S.C. Wang Initial characterization of Fom3 from Streptomyces wedmorensis, the methyltransferase in fosfomycin biosynthesis Arch. Biochem. Biophys. 543 2014 67 73
    • (2014) Arch. Biochem. Biophys. , vol.543 , pp. 67-73
    • Allen, K.D.1    Wang, S.C.2
  • 22
    • 0036867531 scopus 로고    scopus 로고
    • Shewanella denitrificans sp. Nov., A vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea
    • I. Brettar, R. Christen, and M.G. Hofle Shewanella denitrificans sp. nov., a vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea Int. J. Syst. Evol. Microbiol. 52 2002 2211 2217
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 2211-2217
    • Brettar, I.1    Christen, R.2    Hofle, M.G.3
  • 24
    • 0028851951 scopus 로고
    • Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis
    • T. Hidaka, M. Goda, T. Kuzuyama, N. Takei, M. Hidaka, and H. Seto Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis Mol. Gen. Genet. 249 1995 274 280
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 274-280
    • Hidaka, T.1    Goda, M.2    Kuzuyama, T.3    Takei, N.4    Hidaka, M.5    Seto, H.6
  • 25
    • 33846241262 scopus 로고    scopus 로고
    • New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin
    • R.D. Woodyer, G. Li, H. Zhao, and W.A. van der Donk New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin Chem. Commun. (Camb.) 359-361 2007
    • (2007) Chem. Commun. (Camb.) , vol.359-361
    • Woodyer, R.D.1    Li, G.2    Zhao, H.3    Van Der Donk, W.A.4
  • 26
    • 0017036833 scopus 로고
    • Titanium (III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes
    • A.J. Zehnder, and K. Wuhrmann Titanium (III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes Science 194 1976 1165 1166
    • (1976) Science , vol.194 , pp. 1165-1166
    • Zehnder, A.J.1    Wuhrmann, K.2
  • 27
    • 0343036313 scopus 로고    scopus 로고
    • An efficient method for the preparation of methylcobalamin, nature's organometallic methyl transfer catalyst
    • M. Tollinger, T. Derer, R. Konrat, and B. Krautler An efficient method for the preparation of methylcobalamin, nature's organometallic methyl transfer catalyst J. Mol. Catal. 116 1997 147 155
    • (1997) J. Mol. Catal. , vol.116 , pp. 147-155
    • Tollinger, M.1    Derer, T.2    Konrat, R.3    Krautler, B.4
  • 28
    • 0027456586 scopus 로고
    • Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity
    • W.P. Lu, I. Schiau, J.R. Cunningham, and S.W. Ragsdale Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity J. Biol. Chem. 268 1993 5605 5614
    • (1993) J. Biol. Chem. , vol.268 , pp. 5605-5614
    • Lu, W.P.1    Schiau, I.2    Cunningham, J.R.3    Ragsdale, S.W.4
  • 29
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • W.J. Waddell A simple ultraviolet spectrophotometric method for the determination of protein J. Lab. Clin. Med. 48 1956 311 314
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 30
    • 0018065357 scopus 로고
    • Micro methods for the quantitative determination of iron and copper in biological material
    • H. Beinert Micro methods for the quantitative determination of iron and copper in biological material Methods Enzymol. 54 1978 435 445
    • (1978) Methods Enzymol. , vol.54 , pp. 435-445
    • Beinert, H.1
  • 31
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • H. Beinert Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins Anal. Biochem. 131 1983 373 378
    • (1983) Anal. Biochem. , vol.131 , pp. 373-378
    • Beinert, H.1
  • 32
    • 0021686102 scopus 로고
    • Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase
    • M.C. Kennedy, T.A. Kent, M. Emptage, H. Merkle, H. Beinert, and E. Munck Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase J. Biol. Chem. 259 1984 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
  • 33
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form
    • R. Kulzer, T. Pils, R. Kappl, J. Huttermann, and J. Knappe Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form J. Biol. Chem. 273 1998 4897 4903
    • (1998) J. Biol. Chem. , vol.273 , pp. 4897-4903
    • Kulzer, R.1    Pils, T.2    Kappl, R.3    Huttermann, J.4    Knappe, J.5
  • 34
    • 0037432317 scopus 로고    scopus 로고
    • Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB
    • N.B. Ugulava, K.K. Frederick, and J.T. Jarrett Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB Biochemistry 42 2003 2708 2719
    • (2003) Biochemistry , vol.42 , pp. 2708-2719
    • Ugulava, N.B.1    Frederick, K.K.2    Jarrett, J.T.3
  • 35
    • 34547830285 scopus 로고    scopus 로고
    • EPR spectroscopy of the manganese cluster of photosystem II
    • A. Haddy EPR spectroscopy of the manganese cluster of photosystem II Photosynth. Res. 92 2007 357 368
    • (2007) Photosynth. Res. , vol.92 , pp. 357-368
    • Haddy, A.1
  • 36
    • 0021798004 scopus 로고
    • The electron paramagnetic resonance of metalloproteins
    • G. Palmer The electron paramagnetic resonance of metalloproteins Biochem. Soc. Trans. 13 1985 548 560
    • (1985) Biochem. Soc. Trans. , vol.13 , pp. 548-560
    • Palmer, G.1
  • 37
    • 77950368112 scopus 로고    scopus 로고
    • The antiviral protein viperin is a radical SAM enzyme
    • K.S. Duschene, and J.B. Broderick The antiviral protein viperin is a radical SAM enzyme FEBS Lett. 581 2010 1263 1267
    • (2010) FEBS Lett. , vol.581 , pp. 1263-1267
    • Duschene, K.S.1    Broderick, J.B.2
  • 38
    • 70350236635 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biogenesis: Demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-l-methionine enzyme
    • S.R. Wecksler, S. Stoll, H. Tran, O.T. Magnusson, S.P. Wu, D. King, R.D. Britt, and J.P. Klinman Pyrroloquinoline quinone biogenesis: demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-l-methionine enzyme Biochemistry 48 2009 10151 10161
    • (2009) Biochemistry , vol.48 , pp. 10151-10161
    • Wecksler, S.R.1    Stoll, S.2    Tran, H.3    Magnusson, O.T.4    Wu, S.P.5    King, D.6    Britt, R.D.7    Klinman, J.P.8
  • 40
    • 0026483949 scopus 로고
    • Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy
    • R.M. Petrovich, F.J. Ruzicka, G.H. Reed, and P.A. Frey Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy Biochemistry 31 1992 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
  • 41
    • 0342657758 scopus 로고    scopus 로고
    • Electron paramagnetic resonance evidence for a novel interconversion of [3Fe-4S]+ and [4Fe-4S]+ clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activity in vitro
    • A. Lim, and A. Grasland Electron paramagnetic resonance evidence for a novel interconversion of [3Fe-4S]+ and [4Fe-4S]+ clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activity in vitro J. Biol. Chem. 275 2000 12367 12373
    • (2000) J. Biol. Chem. , vol.275 , pp. 12367-12373
    • Lim, A.1    Grasland, A.2
  • 42
    • 36048929198 scopus 로고    scopus 로고
    • Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme
    • S.C. Wang, and P.A. Frey Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme Biochemistry 46 2007 12889 12895
    • (2007) Biochemistry , vol.46 , pp. 12889-12895
    • Wang, S.C.1    Frey, P.A.2
  • 43
    • 13844275460 scopus 로고    scopus 로고
    • Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily
    • C.J. Walsby, D. Ortillo, J. Yang, M.R. Nnyepi, W.E. Broderick, B.M. Hoffman, and J.B. Broderick Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily Inorg. Chem. 44 2005 727 741
    • (2005) Inorg. Chem. , vol.44 , pp. 727-741
    • Walsby, C.J.1    Ortillo, D.2    Yang, J.3    Nnyepi, M.R.4    Broderick, W.E.5    Hoffman, B.M.6    Broderick, J.B.7
  • 44
    • 0037065661 scopus 로고    scopus 로고
    • Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: A Mossbauer spectroscopic study
    • C. Krebs, W.E. Broderick, T.F. Henshaw, J.B. Broderick, and B.H. Huynh Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mossbauer spectroscopic study J. Am. Chem. Soc. 124 2002 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
  • 47
    • 77951930923 scopus 로고    scopus 로고
    • A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
    • T.L. Grove, J.H. Ahlum, P. Sharma, C. Krebs, and S.J. Booker A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters Biochemistry 49 2010 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
  • 48
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • N.B. Ugulava, B.R. Gibney, and J.T. Jarrett Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions Biochemistry 40 2001 8343 8351
    • (2001) Biochemistry , vol.40 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 49
    • 77954859743 scopus 로고
    • Concerning the electrolytic potential of hydrosulphite reactions
    • K. Jellinek Concerning the electrolytic potential of hydrosulphite reactions Z. Elektrochem. Angew. Phys. Chem. 17 1911 157 176
    • (1911) Z. Elektrochem. Angew. Phys. Chem. , vol.17 , pp. 157-176
    • Jellinek, K.1
  • 50
    • 0039713582 scopus 로고
    • The thermodynamic constants of the dithionite (hydrosulfite) ion
    • W.G. McMillan Jr., J.D. Roberts, and C.D. Coryell The thermodynamic constants of the dithionite (hydrosulfite) ion J. Am. Chem. Soc. 64 1942 398 399
    • (1942) J. Am. Chem. Soc. , vol.64 , pp. 398-399
    • McMillan, W.G.1    Roberts, J.D.2    Coryell, C.D.3
  • 51
    • 0016748163 scopus 로고
    • The thermochemical characterization of sodium dithionite, flavin mononucleotide, flavin-adenine dinucleotide and methyl and benzyl viologens as low-potential reductants for biological systems
    • G.D. Watt, and A. Burns The thermochemical characterization of sodium dithionite, flavin mononucleotide, flavin-adenine dinucleotide and methyl and benzyl viologens as low-potential reductants for biological systems Biochem. J. 152 1975 33 37
    • (1975) Biochem. J. , vol.152 , pp. 33-37
    • Watt, G.D.1    Burns, A.2
  • 52
    • 0017886452 scopus 로고
    • - from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase
    • - from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase Eur. J. Biochem. 85 1978 535 547
    • (1978) Eur. J. Biochem. , vol.85 , pp. 535-547
    • Mayhew, S.G.1
  • 53
    • 80055062789 scopus 로고    scopus 로고
    • Cobalamin reduction by dithionite. Evidence for the formation of a six-coordinate cobalamin(II) complex
    • D.S. Salnikov, R. Silaghi-Dumitrescu, S.V. Makarov, R. van Eldik, and G.R. Boss Cobalamin reduction by dithionite. Evidence for the formation of a six-coordinate cobalamin(II) complex Dalton Trans. 40 2012 9831 9834
    • (2012) Dalton Trans. , vol.40 , pp. 9831-9834
    • Salnikov, D.S.1    Silaghi-Dumitrescu, R.2    Makarov, S.V.3    Van Eldik, R.4    Boss, G.R.5
  • 54
    • 0025835066 scopus 로고
    • A method for preparing analytically pure sodium dithionite. Dithionite quality and observed nitrogenase-specific activities
    • C.E. McKenna, W.G. Gutheil, and W. Song A method for preparing analytically pure sodium dithionite. Dithionite quality and observed nitrogenase-specific activities Biochim. Biophys. Acta Gen. Subj. 1075 1991 109 117
    • (1991) Biochim. Biophys. Acta Gen. Subj. , vol.1075 , pp. 109-117
    • McKenna, C.E.1    Gutheil, W.G.2    Song, W.3
  • 55
    • 0025217018 scopus 로고
    • CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres
    • P.A. Lindahl, E. Munck, and S.W. Ragsdale CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres J. Biol. Chem. 265 1990 3873 3879
    • (1990) J. Biol. Chem. , vol.265 , pp. 3873-3879
    • Lindahl, P.A.1    Munck, E.2    Ragsdale, S.W.3
  • 57
    • 0032554639 scopus 로고    scopus 로고
    • Role of the [4Fe-4S] cluster in reductive activation of the cobalt center of the corrinoid iron-sulfur protein from Clostridium thermoaceticum during acetate biosynthesis
    • S. Menon, and S.W. Ragsdale Role of the [4Fe-4S] cluster in reductive activation of the cobalt center of the corrinoid iron-sulfur protein from Clostridium thermoaceticum during acetate biosynthesis Biochemistry 37 1998 5689 5698
    • (1998) Biochemistry , vol.37 , pp. 5689-5698
    • Menon, S.1    Ragsdale, S.W.2
  • 60
    • 0033213404 scopus 로고    scopus 로고
    • Bioactive natural products with carbon-phosphorus bonds and their biosynthesis
    • H. Seto, and T. Kuzuyama Bioactive natural products with carbon-phosphorus bonds and their biosynthesis Nat. Prod. Rep. 16 1999 589 596
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 589-596
    • Seto, H.1    Kuzuyama, T.2
  • 61
    • 0027051383 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 4. the biosynthetic origin of the methyl group of fosfomycin
    • T. Kuzuyama, T. Hidaka, K. Kamigiri, S. Imai, and H. Seto Studies on the biosynthesis of fosfomycin. 4. The biosynthetic origin of the methyl group of fosfomycin J. Antibiot. (Tokyo) 45 1992 1812 1814
    • (1992) J. Antibiot. (Tokyo) , vol.45 , pp. 1812-1814
    • Kuzuyama, T.1    Hidaka, T.2    Kamigiri, K.3    Imai, S.4    Seto, H.5
  • 62
    • 0026050593 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis
    • H. Seto, T. Hidaka, T. Kuzuyama, S. Shibahara, T. Usui, O. Sakanaka, and S. Imai Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis J. Antibiot. (Tokyo) 44 1991 1286 1288
    • (1991) J. Antibiot. (Tokyo) , vol.44 , pp. 1286-1288
    • Seto, H.1    Hidaka, T.2    Kuzuyama, T.3    Shibahara, S.4    Usui, T.5    Sakanaka, O.6    Imai, S.7
  • 64
    • 0034860912 scopus 로고    scopus 로고
    • Cobalamin-dependent methyltransferases
    • R.G. Matthews Cobalamin-dependent methyltransferases Acc. Chem. Res. 34 2001 681 689
    • (2001) Acc. Chem. Res. , vol.34 , pp. 681-689
    • Matthews, R.G.1
  • 65
    • 0001693812 scopus 로고
    • Reductive activation of the methyl-tetrahydromethanopterin:coenzyme M methyl-transferase from Methanobacterium thermoautotrophicum strain H
    • S.W.M. Kengen, J.J. Mosterd, R.L.H. Nelissen, J.T. Keltjens, C. van der Drift, and G.D. Vogels Reductive activation of the methyl-tetrahydromethanopterin:coenzyme M methyl-transferase from Methanobacterium thermoautotrophicum strain H Arch. Microbiol. 150 1988 405 421
    • (1988) Arch. Microbiol. , vol.150 , pp. 405-421
    • Kengen, S.W.M.1    Mosterd, J.J.2    Nelissen, R.L.H.3    Keltjens, J.T.4    Van Der Drift, C.5    Vogels, G.D.6
  • 66
    • 0030752419 scopus 로고    scopus 로고
    • Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli
    • J.T. Jarrett, C.W. Goulding, K. Fluhr, S. Huang, and R.G. Matthews Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli Methods Enzymol. 281 1997 196 213
    • (1997) Methods Enzymol. , vol.281 , pp. 196-213
    • Jarrett, J.T.1    Goulding, C.W.2    Fluhr, K.3    Huang, S.4    Matthews, R.G.5
  • 67
    • 0028172838 scopus 로고
    • N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Catalytic mechanism and sodium ion dependence
    • P. Gartner, D.S. Weiss, U. Harms, and R.K. Thauer N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Catalytic mechanism and sodium ion dependence Eur. J. Biochem. 226 1994 465 472
    • (1994) Eur. J. Biochem. , vol.226 , pp. 465-472
    • Gartner, P.1    Weiss, D.S.2    Harms, U.3    Thauer, R.K.4
  • 68
    • 0026755216 scopus 로고
    • Structural elucidation of two capsular polysaccharides from one strain of Bacteroides fragilis using high-resolution NMR spectroscopy
    • H. Baumann, A.O. Tzianabos, J.R. Brisson, D.L. Kasper, and H.J. Jennings Structural elucidation of two capsular polysaccharides from one strain of Bacteroides fragilis using high-resolution NMR spectroscopy Biochemistry 31 1992 4081 4089
    • (1992) Biochemistry , vol.31 , pp. 4081-4089
    • Baumann, H.1    Tzianabos, A.O.2    Brisson, J.R.3    Kasper, D.L.4    Jennings, H.J.5
  • 69
    • 0034977397 scopus 로고    scopus 로고
    • A novel sphingophosphonolipid head group 1-hydroxy-2-aminoethyl phosphonate in Bdellovibrio stolpii
    • Y. Watanabe, M. Nakajima, T. Hoshino, K. Jayasimhulu, E.E. Brooks, and E.S. Kaneshiro A novel sphingophosphonolipid head group 1-hydroxy-2-aminoethyl phosphonate in Bdellovibrio stolpii Lipids 36 2001 513 519
    • (2001) Lipids , vol.36 , pp. 513-519
    • Watanabe, Y.1    Nakajima, M.2    Hoshino, T.3    Jayasimhulu, K.4    Brooks, E.E.5    Kaneshiro, E.S.6
  • 71
    • 84897510631 scopus 로고    scopus 로고
    • Purification and characterization of phosphonoglycans from Glycomyces sp. Strain NRRL B-16210 and Stackebrandtia nassauensis NRRL B-16338
    • X. Yu, N.P.J. Price, B.S. Evans, and W.W. Metcalf Purification and characterization of phosphonoglycans from Glycomyces sp. Strain NRRL B-16210 and Stackebrandtia nassauensis NRRL B-16338 J. Bacteriol. 196 2014 1768 1779
    • (2014) J. Bacteriol. , vol.196 , pp. 1768-1779
    • Yu, X.1    Price, N.P.J.2    Evans, B.S.3    Metcalf, W.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.