Solid-State NMR of Flavins and Flavoproteins

  • Anne-Frances MillerEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 1146)


Why apply solid-state NMR (SSNMR) to flavins and flavoproteins? NMR provides information on an atom-specific basis about chemical functionality, structure, proximity to other groups, and dynamics of the system. Thus, it has become indispensable to the study of chemicals, materials, catalysts, and biomolecules. It is no surprise then that NMR has a great deal to offer in the study of flavins and flavoenzymes. In general, their catalytic or electron-transfer activity resides essentially in the flavin, a molecule eminently accessible by NMR. However, the specific reactivity displayed depends on a host of subtle interactions whereby the protein biases and reshapes the flavin’s propensities to activate it for one reaction while suppressing other aspects of this cofactor’s prodigious repertoire (Massey et al., J Biol Chem 244:3999–4006, 1969; Müller, Z Naturforsch 27B:1023–1026, 1972; Joosten and van Berkel, Curr Opin Struct Biol 11:195–202, 2007). Thus, we are fascinated to learn about how the flavin cofactor of one enzyme is, and is not, like the flavin cofactor of another. In what follows, we describe how the capabilities of SSNMR can help and are beginning to bear fruit in this exciting endeavor.

Key words

Electronic structure of flavins Solid-state NMR Chemical shift Chemical-shift anisotropy Dipolar coupling Magic-angle spinning Binding motifs 



I am grateful to the NIH for funding under 1 R01 GM085302-01A1 and to Prof. R. G. Griffin for hospitality at the Francis Bitter Magnet Lab (M.I.T.) during my sabbatical. I also thank S. Pyszczynski and E. Munson for assistance in obtaining spectra of MGA, K. Eichele for generously supplying and supporting his software, and T. Maly for help with Fig. 15. This paper is dedicated to my parents on the occasion of my mother’s 80th birthday.


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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of KentuckyLexingtonUSA

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