A mechanism for substrate-Induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase.
Experiments are described to determine the origin of the 6-hydroxyl group of 6-hydroxyFMN produced by the substrate-induced transformation of FMN in the C30A mutant of trimethylamine dehydrogenase. The conversion of FMN to 6-hydroxyFMN is carried out in the presence of H(2)(18)O and 18O(2), and the results clearly show that the 6-hydroxyl group is derived from molecular oxygen and not from water.
Lu
Xingliang
X
Department of Chemistry, Northwestern University, Evanston, IL 60208-3113, USA.
Nikolic
Dejan
D
Mitchell
Deanna J
DJ
van Breemen
Richard B
RB
Mersfelder
John A
JA
Hille
Russ
R
Silverman
Richard B
RB
D019943:Amino Acid Substitution; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005486:Flavin Mononucleotide / Q000031:analogs & derivatives* / Q000096:biosynthesis* / Q000378:metabolism*; D020630:Methylophilus methylotrophus / Q000201:enzymology; D016297:Mutagenesis, Site-Directed; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
C106617:6-hydroxyflavin mononucleotide; D011994:Recombinant Proteins; D005486:Flavin Mononucleotide; D010089:Oxidoreductases, N-Demethylating; C023186:trimethylamine dehydrogenase