Involvement of a flavin iminoquinone methide in the formation of 6-hydroxyflavin mononucleotide in trimethylamine dehydrogenase: a rationale for the existence of 8alpha-methyl and C6-linked covalent flavoproteins

Analysis of the samples of the native and recombinant wild-type trimethylamine dehydrogenases provided the description of the properties of of a trimethylamine dehydrogenase aromatic residue mutant, W355L. Data indicated that the rationale for the existence of 8alpha-methyl and C6-linked covalent flavoproteins is the possible formation of an electrophilic iminoquinone methide in the hydroxylation of flavin.