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Spectrophotometric evidence for a hemoprotein in fish muscle microsomes possible involvement in trimethylamine n oxide tmao demethylase activity


, : Spectrophotometric evidence for a hemoprotein in fish muscle microsomes possible involvement in trimethylamine n oxide tmao demethylase activity. Journal of Agricultural & Food Chemistry 35(1): 34-41

When fish muscle microsomes were reduced with sodium dithionite, characteristic absorption peaks appeared at 444 nm and very faintly at 560 nm. These peaks could also be generated by the presence of some of the components that are required for catalyzing microsomal enzyme-mediated trimethylamine N-oxide (TMAO) demethylation. Under certain conditions, the aborbance peaks underwent reoxidation in the presence of these cofactor components and TMAO. The reducible moiety was identified as protoheme by virtue of its absorption maxima at 557, 532, and 416 nm following solubilization in acid-acetone and reaction with pyridine, and it is proposed that it be named H-444 due to its unique Soret band. Reaction of the microsomes with CO after reduction with dithionite produced a Soret band shift from 444 to 428 nm. The hemin content of the fish muscle microsomes was 0.76 pmol mg-1 protein, some 3 orders of magnitude less than that observed in hepatic microsomes. This microsomal hemoprotein may possibly be involved in TMAO demethylation.

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