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5-(trifluoromethyl)-2'-deoxyuridine 5'-monophosphate (CF3dUMP) inhibits thymidylate synthase (TS) from Lactobacillus casei. In the absence of 5,10-methylenetetrahydrofolate, CF3dUMP binds to the active site of TS and attacks the catalytic nucleophile cysteine 198 to form a covalent complex. Tyrosine 146 and cysteine 198 of the TS are bound covalently to CF3dUMP in the complex.

Thevalidity of the chemically initiated electron exchange luminescence (CIEEL) proposed to explain the bacterial luminescence reaction involving bacterial luciferase was investigated. The study protocol involved the synthesis of various stable 4a,5-dihydroflavin model compounds substituted at the 8-position. The one-electron oxidation potentials of the 4a,5-dihydro forms actas intermediates during catalysis by the flavin-dependent monooxygenase luciferase. The 1-electron oxidation potentials of the model compounds correlated linearly with the corresponding redox potentials, thus supporting the CIEEL.