SUMMARY: Two major trimethylamine--oxide reductases were detected in the periplasmic fraction of the marine bacterium sp. NCMB 400 grown in the presence of trimethylamine -oxide (TMAO). The high- enzyme was purified to homogeneity and consisted of a single polypeptide of 86000 as judged by SDS-PAGE. The second enzyme had an of 47000. On isoelectric focusing, multiple forms of the purified enzyme were revealed with isoelectric points of 5.1 and 5.2. The values for the -oxides of trimethylamine, pyridine and γ-picoline were 0.02, 2.41 and 6.95 mM, respectively. The purified TMAO reductase is a molybdoenzyme containing 1.32 mol Mo (mol enzyme).


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