检测方案
99.9%
形式
rod
制造商/商品名称
Goodfellow 591-685-93
电阻率
5.0 μΩ-cm, 20°C
长度 × 直径
500 m × 10.0 mm
bp
4612 °C (lit.)
mp
2617 °C (lit.)
密度
10.3 g/mL at 25 °C (lit.)
SMILES字符串
[Mo]
InChI
1S/Mo
InChI key
ZOKXTWBITQBERF-UHFFFAOYSA-N
一般描述
For updated SDS information please visit www.goodfellow.com.
法律信息
Product of Goodfellow
法规信息
新产品
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
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
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
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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