1887

Abstract

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 -picoline were 0·02, 2·41 and 6·95 m, respectively. The purified TMAO reductase is a molybdoenzyme containing 1·32 mol Mo (mol enzyme).

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1988-02-01
2021-10-20
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