GF86421584
Molybdenum
wire reel, 200m, diameter 0.2mm, as drawn, 99.95%
Synonym(s):
Molybdenum, MO005135
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About This Item
Empirical Formula (Hill Notation):
Mo
CAS Number:
Molecular Weight:
95.94
MDL number:
UNSPSC Code:
12141727
PubChem Substance ID:
NACRES:
NA.23
Assay
≥99.95%
form
wire
manufacturer/tradename
Goodfellow 864-215-84
resistivity
5.0 μΩ-cm, 20°C
bp
4612 °C (lit.)
mp
2617 °C (lit.)
density
10.3 g/mL at 25 °C (lit.)
SMILES string
[Mo]
InChI
1S/Mo
InChI key
ZOKXTWBITQBERF-UHFFFAOYSA-N
General description
For updated SDS information please visit www.goodfellow.com.
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Manuel Tejada-Jiménez et al.
Metallomics : integrated biometal science, 5(9), 1191-1203 (2013-06-27)
The viability of plants relies on molybdenum, which after binding to the organic moiety of molybdopterin forms the molybdenum cofactor (Moco) and acquires remarkable redox properties. Moco is in the active site of critical molybdoenzymes, which use to work as
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
Ralf R Mendel et al.
Biochimica et biophysica acta, 1823(9), 1568-1579 (2012-03-01)
The transition element molybdenum (Mo) needs to be complexed by a special cofactor in order to gain catalytic activity. With the exception of bacterial Mo-nitrogenase, where Mo is a constituent of the FeMo-cofactor, Mo is bound to a pterin, thus
Guenter Schwarz et al.
Metal ions in life sciences, 13, 415-450 (2014-01-29)
Molybdenum is an essential trace element and crucial for the survival of animals. Four mammalian Mo-dependent enzymes are known, all of them harboring a pterin-based molybdenum cofactor (Moco) in their active site. In these enzymes, molybdenum catalyzes oxygen transfer reactions
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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