Studies on the spin-spin interaction between flavin and iron-sulfur cluster in an iron-sulfur flavoprotein.
When the di- or trimethylamine dehydrogenases (trimethylamine:(acceptor) oxidoreductase (demethylating), EC 1.5.99.7) of certain methylotrophic bacteria are reduced by two electrons with substrate unusual EPR signals arise at g = 2 and g = 4 (Steenkamp, D.J. and Beinert, H. (1982) Biochem. J. 207, 233-239; 241-252) indicative of spin-spin interaction between the FMN and iron-sulfur compounds of these enzymes. An attempt is made to understand, describe and simulate these spectra in terms of a triplet state with possible contributions from both dipolar and anisotropic exchange (J) interactions. No direct measurement of J is available, but various approaches to setting limits to J are outlined. According to these, J approximately 0.4 to 3 cm-1 or 15 to 50 cm-1. The spectra show, in the g = 2 region, a pair of rather sharp inner and a pair of broad outer lines; the latter broaden as well as move out from the center with increasing time (after substrate addition) and substrate concentration, while there is little change of g = 4. The best fits to such spectra were obtained by assuming distribution of D and E values, depending on substrate effects and arriving presumably from 'g-strain'. The fact that both shapes and intensities at g = 2 and g = 4 could be reproduced simultaneously at two frequencies indicates that the assumptions underlying our approaches and interpretations are permissible and reasonable, although we cannot claim their uniqueness. The distance between the centers of the spin densities of the flavin radical and the Fe-S cluster is thought to lie between the limits 3 to 5 A if the asymmetries in the spin-spin interaction are magnetic dipole-dipole in origin. Because there is an indication that the interaction is anisotropic exchange, the upper limit is less stringent.
D001419:Bacteria / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D005415:Flavins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D010084:Oxidation-Reduction; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism; D011487:Protein Conformation
D005415:Flavins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D010089:Oxidoreductases, N-Demethylating; C023186:trimethylamine dehydrogenase