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Molybdenum Biochemistry

The most important role of the molybdenum in living organisms is as a metal heteroatom at the active site in certain enzymes. In nitrogen fixation in certain bacteria, the nitrogenase enzyme, which is involved in the terminal step of reducing molecular nitrogen, usually contains molybdenum in the active site (though replacement of Mo with iron or vanadium is also known). The structure of the catalytic center of the enzyme is similar to that in iron-sulfur proteins: it incorporates a Fe4S3 and multiple MoFe3S3 clusters.

In 2008, evidence was reported that a scarcity of molybdenum in the Earth's early oceans was a limiting factor for nearly two billion years in the further evolution of eukaryotic life (which includes all plants and animals) as eukaryotes cannot fix nitrogen, and must therefore acquire most of their oxidized nitrogen suitable for making organic nitrogen compounds, or the organics themselves (like proteins) from prokaryotic bacteria. The scarcity of molybdenum resulted from the relative lack of oxygen in the early ocean. Most molybdenum compounds have low solubility in water, but the molybdate ion MoO42− is soluble and forms when molybdenum-containing minerals are in contact with oxygen and water. Once oxygen made by early life appeared in seawater, it helped dissolve molybdenum into soluble molybdate from minerals on the sea bottom, making it available for the first time to nitrogen-fixing bacteria, and allowing them to provide more fixed usable nitrogen compounds for higher forms of life.

Although oxygen once promoted nitrogen fixation via making molybdenum available in water, it also directly poisons nitrogenase enzymes. Thus, in Earth's ancient history, after oxygen arrived in large quantities in Earth's air and water, organisms that continued to fix nitrogen in aerobic conditions were required to isolate and protect their nitrogen-fixing enzymes in heterocysts, or similar structures protecting them from too much oxygen. This structural isolation of nitrogen fixation reactions from oxygen in aerobic organisms continues to the present..

Though molybdenum forms compounds with various organic molecules, including carbohydrates and amino acids, it is transported throughout the human body as MoO42−.At least 50 molybdenum-containing enzymes were known by 2002, mostly in bacteria, and their number is increasing with every year;[59][60] those enzymes include aldehyde oxidase, sulfite oxidase and xanthine oxidase. In some animals, and in humans, the oxidation of xanthine to uric acid, a process of purine catabolism, is catalyzed by xanthine oxidase, a molybdenum-containing enzyme. The activity of xanthine oxidase is directly proportional to the amount of molybdenum in the body. However, an extremely high concentration of molybdenum reverses the trend and can act as an inhibitor in both purine catabolism and other processes. Molybdenum concentrations also affect protein synthesis, metabolism and growth.

In animals and plants a tricyclic compound called molybdopterin (which, despite the name, contains no molybdenum) is reacted with molybdate to form a complete molybdenum-containing cofactor called molybdenum cofactor. Save for the phylogenetically-ancient molybdenum nitrogenases discussed above, which fix nitrogen in some bacteria and cyanobacteria, all molybdenum-using enzymes so far identified in nature use the molybdenum cofactor. Molybdenum enzymes in plants and animals catalyze the oxidation and sometimes reduction of certain small molecules, as part of the regulation of nitrogen, sulfur and carbon cycles.

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