Abstract
One of the most essential contributions of selenium to biology is the specialized chemistry performed by selenoproteins. Elucidating the mechanisms by which selenoproteins govern the reactivity of their selenocysteine (Sec) requires exploring how the protein environment primes Sec interactions with substrates, prevents inactivation, and otherwise optimizes the use of this unique amino acid. 77Se nuclear magnetic resonance (NMR) spectroscopy is a particularly powerful technique to study the chemical properties of selenocysteine, its conformational preferences and mobility, and the molecular interactions by which it is stabilized. Recent advances have simplified sample preparation and data analysis, extending the utilization of 77Se in NMR studies of biological samples. These improvements include the development of efficient procedures for enriching proteins with the 77Se isotope, the reports on NMR parameters of different selenoproteins that greatly expand the available basis for data analysis, and the progress in utilizing theoretical calculations for data interpretation. We discuss these areas of progress in 77Se NMR of biological systems, and we consider the range of questions for which 77Se NMR is most useful.
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References
DA Case 2013 Curr Opin Struct Biol 23:172
S Rozovsky 2013 in Biochalcogen Chemistry: The Biological Chemistry of Sulfur, Selenium, and Tellurium, CA Bayse, JL Brumaghim Eds (ACS Press) p 127
SP Davis, FA Jenkins 1951 Phys Rev 83:1269
MH Levitt 2001 Spin dynamics (John Wiley & Sons, England)
JC Facelli 2011 Prog Nucl Magn Reson Spectrosc 58:176
JC Facelli 2004 Conc Magn Reson A 20A:42
D Sitkoff, DA Case 1998 Prog Nucl Magn Reson Spectrosc 32:165
H Duddeck 1995 Prog Nucl Magn Reson Spectrosc 27:1
H Duddeck 2004 Annu Rep NMR Spectrosc 52:105
BA Demko, RE Wasylishen 2009 Prog Nucl Magn Reson Spectrosc 54:208
SA Schaefer et al 2013 J Mol Biol 425:222
M Mobli et al 2009 Angew Chem 48:9312
F Li et al 2014 Proc Natl Acad Sci USA 111:6976
P Gettins, BC Crews 1991 J Biol Chem 266:4804
P Gettins, SA Wardlaw 1991 J Biol Chem 266:3422
NP Luthra et al 1982 J Biol Chem 257:1142
KL House et al 1992 J Am Chem Soc 114:8573
M Mobli et al 2011 Angew Chem 50:11952
J Struppe et al 2015 J Phys Chem B 119:3643
S Schaefer-Ramadan et al 2013 Biochemistry 52:8323
ESJ Arnér et al 1999 J Mol Biol 292:1003
VN Gladyshev et al 1994 Proc Natl Acad Sci USA 91:232
M Salzmann et al 1999 Magn Reson Chem 37:672
PE Dawson et al 1994 Science 266:776
RJ Hondal 2009 Biochim Biophys Acta 1790:1501
B Eckenroth et al 2006 Biochemistry 45:5158
S Schaefer-Ramadan et al 2014 Arch Biochem Biophys 548:60
M Mobli, GF King 2010 Toxicon 56:849
AD de Araujo et al 2012 Angew Chem 51:10298
ESJ Arnér 2010 Exp Cell Res 316:1296
RJ Hondal et al 2013 Antioxid Redox Signal 18:1675
E Oldfield 2005 Philos Trans R Soc London, Ser B 360:1347
K Schmidt-Rohr, HW Spiess 1994 Multidimensional solid-state NMR and polymers (Academic Press, San Diego)
B Han et al 2011 J Biomol NMR 50:43
MP Williamson 2013 Prog Nucl Magn Reson Spectrosc 73:1
OF Lange et al 2012 Proc Natl Acad Sci USA 109:10873
T Helgaker et al 1999 Chem Rev 99:293
JM Griffin et al 2011 J Phys Chem C 115:10859
CA Bayse 2004 Inorg Chem 43:1208
CA Bayse 2005 J Chem Theory Comput 1:1119
CA Bayse, S Antony 2007 Main Group Chem 6:185
Acknowledgements
This work was supported by the Delaware COBRE program with a grant from NIGMS (1 P30 GM110758-01) from the National Institutes of Health and the National Science Foundation under Grant No. MCB-1054447 “CAREER: Reactivity of Selenoproteins” (SR).
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Liu, J., Rozovsky, S. (2016). 77Se NMR Spectroscopy of Selenoproteins. In: Hatfield, D., Schweizer, U., Tsuji, P., Gladyshev, V. (eds) Selenium. Springer, Cham. https://doi.org/10.1007/978-3-319-41283-2_15
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DOI: https://doi.org/10.1007/978-3-319-41283-2_15
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