Molybdenum in biology

[8] In terms of function, molybdoenzymes catalyze the oxidation and sometimes reduction of certain small molecules in the process of regulating nitrogen, sulfur, and carbon.

An extremely high concentration of molybdenum reverses the trend and can inhibit purine catabolism and other processes.

[11][12] Nitrogenases catalyze the production of ammonia from atmospheric nitrogen: The biosynthesis of the FeMoco active site is highly complex.

[21] Although human toxicity data is unavailable, animal studies have shown that chronic ingestion of more than 10 mg/day of molybdenum can cause diarrhea, growth retardation, infertility, low birth weight, and gout; it can also affect the lungs, kidneys, and liver.

[27] Molybdenum deficiency has also been reported as a consequence of non-molybdenum supplemented total parenteral nutrition (complete intravenous feeding) for long periods of time.

It results in high blood levels of sulfite and urate, in much the same way as molybdenum cofactor deficiency.

Ruminants that consume high levels of molybdenum suffer from diarrhea, stunted growth, anemia, and achromotrichia (loss of fur pigment).

It has also been found to have an inhibitory effect on angiogenesis, potentially by inhibiting the membrane translocation process that is dependent on copper ions.

[35] This is a promising avenue for investigation of treatments for cancer, age-related macular degeneration, and other diseases that involve a pathologic proliferation of blood vessels.

A FeMoco cluster with a molybdenum atom in the center
Structure of the FeMoco active site of nitrogenase .
Skeletal structure of a molybdopterin with a single molybdenum atom bound to both of the thiolate groups
The molybdenum cofactor (pictured) is composed of a molybdenum-free organic complex called molybdopterin , which has bound an oxidized molybdenum(VI) atom through adjacent sulfur (or occasionally selenium) atoms. Except for the ancient nitrogenases, all known Mo-using enzymes use this cofactor.