Sources

 Content depends on the concentration of Mo in the

soil

 Found in larger amounts in black beans, walnuts and

lentils

 Also in spinich, lettuce, whole wheat pasta and bread

Absorption, Transport and Storage
 Absorption increases as dietary intake of Mo increases.
(22-1490 µg/day)

 Mo is transported in the blood as molybdate which is

bound to albumin/ alpha-2 macroglobumin

 Mo is found in the tissues as molybdate, free

molybdopterin or molybdopterin bound to enzymes
 Mo can be found in high amounts and concentrations
in the liver, kidneys and the bone.

 Also found in lower amounts and concentrations in

the small intestine, lungs, spleen, brain, thyroid,
adrenal glands and muscle
Functions and Mechanisms of
Action
 Molybdopterin functions as a cofactor for the
metalloenzymes (sulfite oxidase, aldehyde
oxidase, xanthine deydrongenase and xanthine
oxidase)

 It allows for Mo to bind to the catalytic site of the apo-

enzyme

 Molybdopterin carries the Mo to the apoenzyme at its

catalytic site where it undergoes further bonding
 Dioxomolbdopterin is formed as the Mo is further
bonded to 2 Oxygen molecules

 Oxosulfidomolybdopterin is formed as the Mo is

further bonded to one Oxygen and one Sulphur
Sulfite Oxidase
 Located in the mitchondrial inner membrane

 Found in tissues of the heart, liver and kidney

 Contains iron sulphur clusters, 2 molybdopterins in

the dioxo form and 2 cytochrome residues.
 Catalyzes the terminal step in metabolism of
methionine and cysteine. During this process sulfite is
converted to sulfate

 The sulfite may be supplied through the diet because it

is used as an antimicrobial agent during processing.

 The sulfate produced is excreted in the urine or is used

for the synthesis of sulfolipids, sulfoproteins and
mucopolysaccharides
Aldehyde Oxidase
 The enzyme uses the oxosulfido form of
molybdpterin

 Functions in the liver whereby it uses O2 as it

electron acceptor

 Substrates used in this reaction are compounds

containing an aldehyde to generate carboxylic
acids
aldehyde + H2O + O2 <=> a carboxylate + H2O2 + H+
Xanthine Dehydrogenase(XD)
and Xanthine Oxidase(XO)
 Both enzymes are iron dependant which require FAD
and molybdopterin (oxosulfido form)

 XD is found in the tissues in the lungs, intestine, liver

and kidneys

 XO is mainly in the intestines and thyroid cells

 The enzymes are capable of hydroxylating purines,
pyrimidines and other heterocyclic N containing
Compounds

 Hypoxanthine generated from purine catabolism is

oxidized to form xanthine and uric acid

 XD e- are transferred from the substrate to NAD+ to

generate NADH + H+
 XO O2 accepts (e-) from FADH2 and H2O2

 Human disorder known as xanthinuria (Larger amts

of xanthine are excreted in the urine)

 Higher concentrations of xanthine in the urine can

cause the formation of kidney stones
Excretion
 Mo is excreted as molybdate mainly in the urine. It is
excreted in smaller amounts in the feces (with the
interaction Mo of bile), sweat (20µg) and the hair
(0.01µg/g hair)

 Excretion increases as dietary Mo intake increases

 Hence little Mo is absorbed in the body

RDA for Mo
 Infants 0-0.5= 2µg
““““ 0.5-1=3µg
 Children 4-8= 22µg
 Male and Female 9-13= 34µg
 “ “ “ “ “ “ “ “ 14-18= 43µg
 “ “ “ “ “ “ “ “ 19- >70= 45µg
 Pregnant women = 50µg
Deficiency
 In China it has been documented with low Mo has
been linked with esophageal cancer

 Congenital Mo cofactor deficiency disease in infants

disrupts the body’s use of Mo in the metalloenzymes
Toxicity
 Mo is relatively non toxic with intakes of 1500µg per
day.

 Possible to experience syntoms of gout (accumulation

of uric acid in the joints resulting in inflammation)

 Occurs due to high concentrations of uric acid from

XO and XD activity
References
 http://minerals.usgs.gov/minerals/pubs/commodity/
molybdenum/

 http://www.lenntech.com/periodic/elements/mo.htm
 http://www.cancer.org/Treatment/TreatmentsandSide
Effects/ComplementaryandAlternativeMedicine/Herb
sVitaminsandMinerals/molybdenum