Metalloproteins: Radical SAM catalysis via an organometallic intermediate with an Fe-[5′-C]-deoxyadenosyl bond

Science

Volumn 352, Issue 6287, 2016, Pages 822-825

  Horitani, Masaki ^a   Shisler, Krista ^b   Broderick, William E ^b   Hutcheson, Rachel U ^b   Duschene, Kaitlin S ^b   Marts, Amy R ^a   Hoffman, Brian M ^a   Broderick, Joan B ^b  

^a NORTHWESTERN UNIVERSITY   (United States)

^b MONTANA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; COBAMAMIDE; COORDINATION COMPOUND; ENZYME; IRON 57; IRON COMPLEX; PYRUVATE FORMATE LYASE ACTIVATING ENZYME; RADICAL; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG; [5' C] DEOXYADENOSYL; CYANOCOBALAMIN; IRON SULFUR PROTEIN; ORGANOMETALLIC COMPOUND; PYRUVATE FORMATE-LYASE ACTIVATING ENZYME;

CATALYSIS; CHEMICAL BONDING; ELECTRON; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; IRON; PROTEIN; RADICAL;

AMPLITUDE MODULATION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; COVALENT BOND; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTRON SPIN RESONANCE; ENZYME MECHANISM; PRIORITY JOURNAL; RADICAL REACTION; REACTION ANALYSIS; BIOCATALYSIS; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE;

BIOCATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES; IRON-SULFUR PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; ORGANOMETALLIC COMPOUNDS; S-ADENOSYLMETHIONINE; VITAMIN B 12;

EID: 84969203984     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf5327     Document Type: Article

References (26)

1. J. B. Broderick, B. R. Duffus, K. S. Duschene, E. M. Shepard, Chem. Rev. 114, 4229-4317 (2014).
2. G. Sicoli et al., Science 351, 1320-1323 (2016).
3. C. J. Walsby, D. Ortillo, W. E. Broderick, J. B. Broderick, B. M. Hoffman, J. Am. Chem. Soc. 124, 11270-11271 (2002).
4. D. Chen, C. Walsby, B. M. Hoffman, P. A. Frey, J. Am. Chem. Soc. 125, 11788-11789 (2003).
5. J. L. Vey et al., Proc. Natl. Acad. Sci. U.S.A. 105, 16137-16141 (2008).
6. B. W. Lepore, F. J. Ruzicka, P. A. Frey, D. Ringe, Proc. Natl. Acad. Sci. U.S.A. 102, 13819-13824 (2005).
7. O. T. Magnusson, G. H. Reed, P. A. Frey, J. Am. Chem. Soc. 121, 9764-9765 (1999).
8. O. T. Magnusson, G. H. Reed, P. A. Frey, Biochemistry 40, 7773-7782 (2001).
9. M. Horitani et al., J. Am. Chem. Soc. 137, 7111-7121 (2015).
10. K. A. Shisler, J. B. Broderick, Arch. Biochem. Biophys. 546, 64-71 (2014).
11. C. J. Walsby et al., J. Am. Chem. Soc. 124, 3143-3151 (2002).
12. A. F. V. Wagner, M. Frey, F. A. Neugebauer, W. Schäfer, J. Knappe, Proc. Natl. Acad. Sci. U.S.A. 89, 996-1000 (1992).
13. M. Sivaraja, D. B. Goodin, M. Smith, B. M. Hoffman, Science 245, 738-740 (1989).
14. A. L. P. Houseman, P. E. Doan, D. B. Goodwin, B. M. Hoffman, Biochemistry 32, 4430-4443 (1993).
15. J. E. Huyett et al., J. Am. Chem. Soc. 117, 9033-9041 (1995).
16. H. M. McConnell, R. W. Fessenden, J. Chem. Phys. 31, 1688 (1959).
17. T. Cole, C. Heller, J. Chem. Phys. 34, 1085 (1961).
18. R. Banerjee, Chem. Rev. 103, 2083-2094 (2003).
19. K. L. Brown, Chem. Rev. 105, 2075-2150 (2005).
20. A. Becker et al., Nat. Struct. Mol. Biol. 6, 969-975 (1999).
21. Y. Peng, S. E. Veneziano, G. D. Gillispie, J. B. Broderick, J. Biol. Chem. 285, 27224-27231 (2010).
22. W. Lubitz, H. Ogata, O. Rüdiger, E. Reijerse, Chem. Rev. 114, 4081-4148 (2014).
23. G. E. Cutsail III, J. Telser, B. M. Hoffman, Biochim. Biophys. Acta 1853, 1370-1394 (2015).
24. H.-I. Lee et al., J. Am. Chem. Soc. 126, 9563-9569 (2004).
25. W. Xu et al., Biochemistry 51, 4835-4849 (2012).
26. I. Span et al., J. Am. Chem. Soc. 136, 7926-7932 (2014).