-
1
-
-
37649002924
-
Gene family encoding the major toxins of lethal Amanita mushrooms
-
Hallen, H.E., Luo, H., Scott-Craig, J.S. & Walton, J.D. Gene family encoding the major toxins of lethal Amanita mushrooms. Proc. Natl. Acad. Sci. USA 104, 19097-19101 (2007).
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 19097-19101
-
-
Hallen, H.E.1
Luo, H.2
Scott-Craig, J.S.3
Walton, J.D.4
-
2
-
-
78049323503
-
Naturally occurring circular proteins: Distribution, biosynthesis and evolution
-
Cascales, L. & Craik, D.J. Naturally occurring circular proteins: distribution, biosynthesis and evolution. Org. Biomol. Chem. 8, 5035-5047 (2010).
-
(2010)
Org. Biomol. Chem.
, vol.8
, pp. 5035-5047
-
-
Cascales, L.1
Craik, D.J.2
-
3
-
-
37349105310
-
Genetic features of circular bacteriocins produced by Gram-positive bacteria
-
DOI 10.1111/j.1574-6976.2007.00087.x
-
Maqueda, M. et al. Genetic features of circular bacteriocins produced by Gram-positive bacteria. FEMS Microbiol. Rev. 32, 2-22 (2008). (Pubitemid 350293913)
-
(2008)
FEMS Microbiology Reviews
, vol.32
, Issue.1
, pp. 2-22
-
-
Maqueda, M.1
Sanchez-Hidalgo, M.2
Fernandez, M.3
Montalban-Lopez, M.4
Valdivia, E.5
Martinez-Bueno, M.6
-
4
-
-
0022413987
-
Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: Isolation, structural analysis, and biogenesis
-
Babasaki, K., Takao, T., Shimonishi, Y. & Kurahashi, K. Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis. J. Biochem. 98, 585-603 (1985). (Pubitemid 16216406)
-
(1985)
Journal of Biochemistry
, vol.98
, Issue.3
, pp. 585-603
-
-
Babasaki, K.1
Takao, T.2
Shimonishi, Y.3
Kurahashi, K.4
-
5
-
-
33947518267
-
The spectrum of antimicrobial activity of the bacteriocin subtilosin A
-
DOI 10.1093/jac/dkl495
-
Shelburne, C.E. et al. The spectrum of antimicrobial activity of the bacteriocin subtilosin A. J. Antimicrob. Chemother. 59, 297-300 (2007). (Pubitemid 47072070)
-
(2007)
Journal of Antimicrobial Chemotherapy
, vol.59
, Issue.2
, pp. 297-300
-
-
Shelburne, C.E.1
An, F.Y.2
Dholpe, V.3
Ramamoorthy, A.4
Lopatin, D.E.5
Lantz, M.S.6
-
6
-
-
54249143112
-
Spermicidal activity of the safe natural antimicrobial peptide subtilosin
-
Sutyak, K.E. et al. Spermicidal activity of the safe natural antimicrobial peptide subtilosin. Infect. Dis. Obstet. Gynecol. 2008, 540758 (2008).
-
(2008)
Infect. Dis. Obstet. Gynecol. 2008
, pp. 540758
-
-
Sutyak, K.E.1
-
7
-
-
43549117478
-
Spermicidal bacteriocins: Lacticin 3147 and subtilosin A
-
DOI 10.1016/j.bmcl.2007.11.024, PII S0960894X07013352
-
Silkin, L., Hamza, S., Kaufman, S., Cobb, S.L. & Vederas, J.C. Spermicidal bacteriocins: lacticin 3147 and subtilosin A. Bioorg. Med. Chem. Lett. 18, 3103-3106 (2008). (Pubitemid 351680380)
-
(2008)
Bioorganic and Medicinal Chemistry Letters
, vol.18
, Issue.10
, pp. 3103-3106
-
-
Silkin, L.1
Hamza, S.2
Kaufman, S.3
Cobb, S.L.4
Vederas, J.C.5
-
8
-
-
69949088377
-
Isolation of a variant of subtilosin A with hemolytic activity
-
Huang, T. et al. Isolation of a variant of subtilosin A with hemolytic activity. J. Bacteriol. 191, 5690-5696 (2009).
-
(2009)
J. Bacteriol.
, vol.191
, pp. 5690-5696
-
-
Huang, T.1
-
9
-
-
0037462081
-
Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine
-
DOI 10.1021/ja029654t
-
Kawulka, K. et al. Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine. J. Am. Chem. Soc. 125, 4726-4727 (2003). (Pubitemid 36505362)
-
(2003)
Journal of the American Chemical Society
, vol.125
, Issue.16
, pp. 4726-4727
-
-
Kawulka, K.1
Sprules, T.2
McKay, R.T.3
Mercier, P.4
Diaper, C.M.5
Zuber, P.6
Vederas, J.C.7
-
10
-
-
1642367862
-
Structure of Subtilosin A, A Cyclic Antimicrobial Peptide from Bacillus subtilis with Unusual Sulfur to α-Carbon Cross-Links: Formation and Reduction of α-Thio-α-Amino Acid Derivatives
-
DOI 10.1021/bi0359527
-
Kawulka, K.E. et al. Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to α-carbon cross-links: formation and reduction of α-thio-α-amino acid derivatives. Biochemistry 43, 3385-3395 (2004). (Pubitemid 38391695)
-
(2004)
Biochemistry
, vol.43
, Issue.12
, pp. 3385-3395
-
-
Kawulka, K.E.1
Sprules, T.2
Diaper, C.M.3
Whittal, R.M.4
McKay, R.T.5
Mercier, P.6
Zuber, P.7
Vederas, J.C.8
-
11
-
-
77957977117
-
Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis
-
Liu, W.-T. et al. Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 107, 16286-16290 (2010).
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 16286-16290
-
-
Liu, W.-T.1
-
12
-
-
70349234326
-
Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361
-
Lee, H., Churey, J.J. & Worobo, R.W. Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361. FEMS Microbiol. Lett. 299, 205-213 (2009).
-
(2009)
FEMS Microbiol. Lett.
, vol.299
, pp. 205-213
-
-
Lee, H.1
Churey, J.J.2
Worobo, R.W.3
-
13
-
-
80052485163
-
The 3D solution structure of thurincin H, a cacteriocin with four sulfur to α-carbon crosslinks
-
Sit, C.S., van Belkum, M.J., McKay, R.T., Worobo, R.W. & Vederas, J.C. The 3D solution structure of thurincin H, a cacteriocin with four sulfur to α-carbon crosslinks. Angew. Chem. Int. Edn Engl. 50, 8718-8721 (2011).
-
(2011)
Angew. Chem. Int. Edn Engl.
, vol.50
, pp. 8718-8721
-
-
Sit, C.S.1
Van Belkum, M.J.2
McKay, R.T.3
Worobo, R.W.4
Vederas, J.C.5
-
14
-
-
77952679997
-
Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against clostridium difficile
-
Rea, M.C. et al. Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile. Proc. Natl. Acad. Sci. USA 107, 9352-9357 (2010).
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 9352-9357
-
-
Rea, M.C.1
-
15
-
-
79957690316
-
The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links
-
Sit, C.S., McKay, R.T., Hill, C., Ross, R.P. & Vederas, J.C. The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links. J. Am. Chem. Soc. 133, 7680-7683 (2011).
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 7680-7683
-
-
Sit, C.S.1
McKay, R.T.2
Hill, C.3
Ross, R.P.4
Vederas, J.C.5
-
16
-
-
0032726081
-
Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin
-
Zheng, G., Yan, L.Z., Vederas, J.C. & Zuber, P. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J. Bacteriol. 181, 7346-7355 (1999).
-
(1999)
J. Bacteriol.
, vol.181
, pp. 7346-7355
-
-
Zheng, G.1
Yan, L.Z.2
Vederas, J.C.3
Zuber, P.4
-
17
-
-
0034039083
-
Mutational analysis of the sbo-alb locus of Bacillus subtilis: Identification of genes required for subtilosin production and immunity
-
DOI 10.1128/JB.182.11.3266-3273.2000
-
Zheng, G., Hehn, R. & Zuber, P. Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity. J. Bacteriol. 182, 3266-3273 (2000). (Pubitemid 30326945)
-
(2000)
Journal of Bacteriology
, vol.182
, Issue.11
, pp. 3266-3273
-
-
Zheng, G.1
Hehn, R.2
Zuber, P.3
-
18
-
-
0034087235
-
Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis
-
DOI 10.1128/JB.182.11.3274-3277.2000
-
Nakano, M.M., Zheng, G. & Zuber, P. Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis. J. Bacteriol. 182, 3274-3277 (2000). (Pubitemid 30326946)
-
(2000)
Journal of Bacteriology
, vol.182
, Issue.11
, pp. 3274-3277
-
-
Nakano, M.M.1
Zheng, G.2
Zuber, P.3
-
19
-
-
14644396519
-
The rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions
-
DOI 10.1128/JB.187.6.2010-2019.2005
-
Albano, M. et al. The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions. J. Bacteriol. 187, 2010-2019 (2005). (Pubitemid 40316231)
-
(2005)
Journal of Bacteriology
, vol.187
, Issue.6
, pp. 2010-2019
-
-
Albano, M.1
Smits, W.K.2
Ho, L.T.Y.3
Kraigher, B.4
Mandic-Mulec, I.5
Kuipers, O.P.6
Dubnau, D.7
-
20
-
-
0042366189
-
Cannibalism by sporulating bacteria
-
DOI 10.1126/science.1086462
-
González-Pastor, J.E., Hobbs, E.C. & Losick, R. Cannibalism by sporulating bacteria. Science 301, 510-513 (2003). (Pubitemid 36900307)
-
(2003)
Science
, vol.301
, Issue.5632
, pp. 510-513
-
-
Gonzalez-Pastor, J.E.1
Hobbs, E.C.2
Losick, R.3
-
21
-
-
0035282866
-
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., Reyes-Spindola, J. & Miller, N. 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 (2001). (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
-
22
-
-
39849096603
-
The radical SAM superfamily
-
DOI 10.1080/10409230701829169, PII 791049421
-
Frey, P.A., Hegeman, A.D. & Ruzicka, F.J. The radical SAM superfamily. Crit. Rev. Biochem. Mol. Biol. 43, 63-88 (2008). (Pubitemid 351315858)
-
(2008)
Critical Reviews in Biochemistry and Molecular Biology
, vol.43
, Issue.1
, pp. 63-88
-
-
Frey, P.A.1
Hegeman, A.D.2
Ruzicka, F.J.3
-
23
-
-
65249089666
-
Control of radical chemistry in the AdoMet radical enzymes
-
Duschene, K.S., Veneziano, S.E., Silver, S.C. & Broderick, J.B. Control of radical chemistry in the AdoMet radical enzymes. Curr. Opin. Chem. Biol. 13, 74-83 (2009).
-
(2009)
Curr. Opin. Chem. Biol.
, vol.13
, pp. 74-83
-
-
Duschene, K.S.1
Veneziano, S.E.2
Silver, S.C.3
Broderick, J.B.4
-
24
-
-
0014939344
-
Lysine 2,3-aminomutase purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme
-
Chirpich, T.P., Zappia, V., Costilow, R.N. & Barker, H.A. Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme. J. Biol. Chem. 245, 1778-1789 (1970).
-
(1970)
J. Biol. Chem.
, vol.245
, pp. 1778-1789
-
-
Chirpich, T.P.1
Zappia, V.2
Costilow, R.N.3
Barker, H.A.4
-
25
-
-
27644450582
-
Structural and functional comparison on HemN to other radical SAM enzymes
-
DOI 10.1515/BC.2005.113
-
Layer, G. et al. Structural and functional comparison of HemN to other radical SAM enzymes. Biol. Chem. 386, 971-980 (2005). (Pubitemid 41548729)
-
(2005)
Biological Chemistry
, vol.386
, Issue.10
, pp. 971-980
-
-
Layer, G.1
Kervio, E.2
Morlock, G.3
Heinz, D.W.4
Jahn, D.5
Retey, J.6
Schubert, W.-D.7
-
26
-
-
0031577321
-
Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical
-
DOI 10.1006/bbrc.1997.6952
-
Guianvarc'h, D., Florentin, D., Tse Sum Bui, B., Nunzi, F. & Marquet, A. Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical. Biochem. Biophys. Res. Commun. 236, 402-406 (1997). (Pubitemid 27373308)
-
(1997)
Biochemical and Biophysical Research Communications
, vol.236
, Issue.2
, pp. 402-406
-
-
Guianvarc'h, D.1
Florentin, D.2
Bui, B.T.S.3
Nunzi, F.4
Marquet, A.5
-
27
-
-
0035902569
-
Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
-
DOI 10.1021/bi0104625
-
Ugulava, N.B., Gibney, B.R. & Jarrett, J.T. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 40, 8343-8351 (2001). (Pubitemid 32661895)
-
(2001)
Biochemistry
, vol.40
, Issue.28
, pp. 8343-8351
-
-
Ugulava, N.B.1
Gibney, B.R.2
Jarrett, J.T.3
-
28
-
-
0346727529
-
Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
-
DOI 10.1126/science.1088493
-
Berkovitch, F. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303, 76-79 (2004). (Pubitemid 38055773)
-
(2004)
Science
, vol.303
, Issue.5654
, pp. 76-79
-
-
Berkovitch, F.1
Nicolet, Y.2
Wan, J.T.3
Jarrett, J.T.4
Drennan, C.L.5
-
29
-
-
0034642248
-
Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
-
Miller, J.R. et al. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39, 15166-15178 (2000).
-
(2000)
Biochemistry
, vol.39
, pp. 15166-15178
-
-
Miller, J.R.1
-
30
-
-
2542641045
-
Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid
-
DOI 10.1021/bi049528x
-
Cicchillo, R.M. et al. Lipoyl synthase requires two equivalents of S-adenosyl-l-methionine to synthesize one equivalent of lipoic acid. Biochemistry 43, 6378-6386 (2004). (Pubitemid 38697537)
-
(2004)
Biochemistry
, vol.43
, Issue.21
, pp. 6378-6386
-
-
Cicchillo, R.M.1
Iwig, D.F.2
Jones, A.D.3
Nesbitt, N.M.4
Baleanu-Gogonea, C.5
Souder, M.G.6
Tu, L.7
Booker, S.J.8
-
31
-
-
1942501738
-
The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor
-
DOI 10.1074/jbc.M311815200
-
Santamaria-Araujo, J.A. et al. The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor. J. Biol. Chem. 279, 15994-15999 (2004). (Pubitemid 38509288)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.16
, pp. 15994-15999
-
-
Santamaria-Araujo, J.A.1
Fischer, B.2
Otte, T.3
Nimtz, M.4
Mendel, R.R.5
Wray, V.6
Schwarz, G.7
-
32
-
-
33646468635
-
Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
-
Hänzelmann, P. & Schindelin, H. 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. USA 103, 6829-6834 (2006).
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 6829-6834
-
-
Hänzelmann, P.1
Schindelin, H.2
-
33
-
-
9144220291
-
MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
-
DOI 10.1074/jbc.M408562200
-
Pierrel, F., Douki, T., Fontecave, M. & Atta, M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J. Biol. Chem. 279, 47555-47563 (2004). (Pubitemid 39540900)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.46
, pp. 47555-47563
-
-
Pierrel, F.1
Douki, T.2
Fontecave, M.3
Atta, M.4
-
34
-
-
34247631048
-
MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters
-
DOI 10.1021/bi7000449
-
Hernández, H.L. et al. MiaB, a bifunctional radical-S- adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 46, 5140-5147 (2007). (Pubitemid 46683012)
-
(2007)
Biochemistry
, vol.46
, Issue.17
, pp. 5140-5147
-
-
Hernandez, H.L.1
Pierrel, F.2
Elleingand, E.3
Garcia-Serres, R.4
Huynh, B.H.5
Johnson, M.K.6
Fontecave, M.7
Atta, M.8
-
35
-
-
70350215875
-
Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily
-
Lee, K.-H. et al. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry 48, 10162-10174 (2009).
-
(2009)
Biochemistry
, vol.48
, pp. 10162-10174
-
-
Lee, K.-H.1
-
36
-
-
37049024768
-
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. & Eguchi, T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J. Am. Chem. Soc. 129, 15147-15155 (2007). (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
-
37
-
-
77951930923
-
A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
-
Grove, T.L., Ahlum, J.H., Sharma, P., Krebs, C. & Booker, S.J. A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters. Biochemistry 49, 3783-3785 (2010).
-
(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
-
38
-
-
2442499333
-
Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB
-
DOI 10.1074/jbc.M313855200
-
Fang, Q., Peng, J. & Dierks, T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. J. Biol. Chem. 279, 14570-14578 (2004). (Pubitemid 38618844)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.15
, pp. 14570-14578
-
-
Fang, Q.1
Peng, J.2
Dierks, T.3
-
39
-
-
47349101467
-
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
-
DOI 10.1021/bi8004297
-
Grove, T.L., Lee, K.-H., St. Clair, J., Krebs, C. & Booker, S.J. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry 47, 7523-7538 (2008). (Pubitemid 351994313)
-
(2008)
Biochemistry
, vol.47
, Issue.28
, pp. 7523-7538
-
-
Grove, T.L.1
Lee, K.-H.2
St. Clair, J.3
Krebs, C.4
Booker, S.J.5
-
40
-
-
0020766701
-
Synthetic routes to iron sulfide (Fe2S2, Fe3S4, Fe4S4, and Fe6S9), clusters from the common precursor tetrakis(ethanethiolate)ferrate2- ion ([Fe(SC2H5)4]2-): Structures and properties of [Fe3S4(SR)4]3- and bis(ethanethiolate)nonathioxohexaferrate4- ion ([Fe6S9(SC2H5)2]4-), examples of the newest types of Fe-S-SR clusters
-
Hagen, K. & Watson, A. Synthetic routes to iron sulfide (Fe2S2, Fe3S4, Fe4S4, and Fe6S9), clusters from the common precursor tetrakis(ethanethiolate)ferrate2- ion ([Fe(SC2H5)4]2-): structures and properties of [Fe3S4(SR)4]3- and bis(ethanethiolate)nonathioxohexaferrate4- ion ([Fe6S9(SC2H5)2]4-), examples of the newest types of Fe-S-SR clusters. J. Am. Chem. Soc. 105, 3905-3913 (1983).
-
(1983)
J. Am. Chem. Soc.
, vol.105
, pp. 3905-3913
-
-
Hagen, K.1
Watson, A.2
-
41
-
-
0038434902
-
Reconstitution and characterization of the Polynuclear Iron-Sulfur cluster in pyruvate formate-lyase-activating enzyme: Molecular properties of the holoenzyme form
-
DOI 10.1074/jbc.273.9.4897
-
Külzer, R., Pils, T., Kappl, R., Hüttermann, J. & Knappe, J. 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, 4897-4903 (1998). (Pubitemid 28108640)
-
(1998)
Journal of Biological Chemistry
, vol.273
, Issue.9
, pp. 4897-4903
-
-
Kulzer, R.1
Pils, T.2
Kappl, R.3
Huttermann, J.4
Knappe, J.5
-
42
-
-
0034595376
-
Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters
-
DOI 10.1021/bi9926227
-
Ugulava, N.B., Gibney, B.R. & Jarrett, J.T. Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters. Biochemistry 39, 5206-5214 (2000). (Pubitemid 30241643)
-
(2000)
Biochemistry
, vol.39
, Issue.17
, pp. 5206-5214
-
-
Ugulava, N.B.1
Gibney, B.R.2
Jarrett, J.T.3
-
43
-
-
77950368112
-
The antiviral protein viperin is a radical SAM enzyme
-
Duschene, K.S. & Broderick, J.B. The antiviral protein viperin is a radical SAM enzyme. FEBS Lett. 584, 1263-1267 (2010).
-
(2010)
FEBS Lett.
, vol.584
, pp. 1263-1267
-
-
Duschene, K.S.1
Broderick, J.B.2
-
44
-
-
56249110190
-
Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily
-
Chatterjee, A. et al. Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily. Nat. Chem. Biol. 4, 758-765 (2008).
-
(2008)
Nat. Chem. Biol.
, vol.4
, pp. 758-765
-
-
Chatterjee, A.1
-
45
-
-
79960080501
-
Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters
-
Murphy, K. et al. Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters. PLoS ONE 6, e20852 (2011).
-
(2011)
PLoS ONE
, vol.6
-
-
Murphy, K.1
-
46
-
-
74049115080
-
Follow the leader: The use of leader peptides to guide natural product biosynthesis
-
Oman, T.J. & van der Donk, W.A. Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat. Chem. Biol. 6, 9-18 (2010).
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 9-18
-
-
Oman, T.J.1
Van Der Donk, W.A.2
-
47
-
-
0942268866
-
Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
-
DOI 10.1126/science.1092600
-
Xie, L., Miller, L., Chatterjee, C. & Averin, O. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity. Science 303, 679-681 (2004). (Pubitemid 38141635)
-
(2004)
Science
, vol.303
, Issue.5658
, pp. 679-681
-
-
Xie, L.1
Miller, L.M.2
Chatterjee, C.3
Averin, O.4
Kelleher, N.L.5
Van Der Donk, W.A.6
-
48
-
-
14844340728
-
Biosynthesis and mode of action of lantibiotics
-
Chatterjee, C., Paul, M., Xie, L. & van der Donk, W.A. Biosynthesis and mode of action of lantibiotics. Chem. Rev. 105, 633-684 (2005).
-
(2005)
Chem. Rev.
, vol.105
, pp. 633-684
-
-
Chatterjee, C.1
Paul, M.2
Xie, L.3
Van Der Donk, W.A.4
-
49
-
-
0030947388
-
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
-
DOI 10.1038/42990
-
Roach, P.L., Clifton, I., Hensgens, C. & Shibata, N. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827-830 (1997). (Pubitemid 27270911)
-
(1997)
Nature
, vol.387
, Issue.6635
, pp. 827-830
-
-
Roach, P.L.1
Clifton, I.J.2
Hensgens, C.M.H.3
Shibata, N.4
Schofield, C.J.5
Hajdu, J.6
Baldwin, J.E.7
-
50
-
-
0037072870
-
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
-
Layer, G., Verfürth, K., Mahlitz, E. & Jahn, D. Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J. Biol. Chem. 277, 34136-34142 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 34136-34142
-
-
Layer, G.1
Verfürth, K.2
Mahlitz, E.3
Jahn, D.4
|