Biochemical properties of molybdenum cofactor isolated from fish liver.

Abstract

Recent studies have demonstrated that the fish liver protein fraction extract obtained by gel filtration exhibits nitric oxide synthase (NOS)-independent NO synthase from nitrates and nitrites. This activity was attributed to the molybdenum enzymes (Mo-enzymes) group which was already demonstrated in mammals. However, the evidence that NOS-independent NO synthase activity can be classified as a fish Mo-enzyme has been poorly demonstrated. In mammals, Mo-enzymes NOS-independent NO synthase activity occurs at the molybdenum center. We studied the ability of molybdenum cofactor (Mo-co) isolated from the protein fraction of fish liver extract to restore the NADPH-nitrate reductase (NADPH-NR) activity from Neurospora crassa nit-1. Our results demonstrated that Mo-co from the extract from fish liver was able to recover NADPH-NR activity in the extract of N. crassa nit-1, thereby possessing the ability to reduce nitrogen compounds. However, the oxidation of Mo-co from fish liver destabilizes molybdenum, leading to its inactivation. However, the results obtained under anaerobic conditions with dithionite indicate that Mo remains bound to Mo-co under highly reducing conditions. This may also indicate that the availability of Mo is not the sole factor affecting the activity of Mo-enzymes, also oxygen content after the synthesis of mature Mo-co may play a role in cofactor inactivation.