ArticleFish physiology and biochemistry2025
Biochemical properties of molybdenum cofactor isolated from fish liver.
Article in Fish physiology and biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- The biological relevance of potentially toxic metals in freshwater fish.Frontiers in physiology · 2025Review
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9 authors.
Funding
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.
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