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.
|Number of pages||34|
|Journal||Methods in Molecular Biology|
|State||Published - 2014|
Bibliographical notePublisher Copyright:
© Springer Science+Business Media New York 2014.
- Binding motifs
- Chemical shift
- Chemical-shift anisotropy
- Dipolar coupling
- Electronic structure of flavins
- Magic-angle spinning
- Solid-state NMR
ASJC Scopus subject areas
- Molecular Biology