InChI
1S/Mo
SMILES string
[Mo]
InChI key
ZOKXTWBITQBERF-UHFFFAOYSA-N
assay
≥99.95%
form
wire
manufacturer/tradename
Goodfellow 902-613-67
resistivity
5.0 μΩ-cm, 20°C
bp
4612 °C (lit.)
mp
2617 °C (lit.)
density
10.3 g/mL at 25 °C (lit.)
General description
For updated SDS information please visit www.goodfellow.com.
Legal Information
Product of Goodfellow
法规信息
新产品
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Mohammad-Reza Rashidi et al.
Expert opinion on drug metabolism & toxicology, 6(2), 133-152 (2010-01-26)
Molybdenum hydroxylases, aldehyde oxidase and xanthine oxidase, are metalloflavoproteins that catalyze both oxidation and reduction of a broad range of drugs and other xenobiotics indicating the importance of these enzymes in drug oxidation, detoxification and activation. Both enzymes are also
Maria Lyra et al.
Hellenic journal of nuclear medicine, 14(1), 49-55 (2011-04-23)
The sleeping giant of molybdenum-99 ((99)Mo) production is grinding to a halt and the world is wondering how this happened. Fewer than 10 reactors in the world are capable of producing radio nuclides for medicine; approximately 50% of the world's
Ralf R Mendel
BioFactors (Oxford, England), 35(5), 429-434 (2009-07-23)
The transition element molybdenum (Mo) is an essential micronutrient that is needed as catalytically active metal during enzyme catalysis. In humans four enzymes depend on Mo: sulfite oxidase, xanthine oxidoreductase, aldehyde oxidase, and mitochondrial amidoxime reductase. In addition to these
Angel Llamas et al.
Metallomics : integrated biometal science, 3(6), 578-590 (2011-05-31)
Molybdenum (Mo) is a very scarce element whose function is fundamental in living beings within the active site of Mo-oxidoreductases, playing key roles in the metabolism of N, S, purines, hormone biosynthesis, transformation of drugs and xenobiotics, etc. In eukaryotes
Yilin Hu et al.
Microbiology and molecular biology reviews : MMBR, 75(4), 664-677 (2011-12-01)
Nitrogenase catalyzes a key step in the global nitrogen cycle, the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is a substantial amount of interest in elucidating the biosynthetic mechanisms of the FeMoco and the P-cluster of nitrogenase, because
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