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47895-41-0

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47895-41-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 47895-41-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,7,8,9 and 5 respectively; the second part has 2 digits, 4 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 47895-41:
(7*4)+(6*7)+(5*8)+(4*9)+(3*5)+(2*4)+(1*1)=170
170 % 10 = 0
So 47895-41-0 is a valid CAS Registry Number.

47895-41-0Relevant articles and documents

Nickel-cysteine binding supported by phosphine chelates

Desrochers, Patrick J.,Duong, Davis S.,Marshall, Ariel S.,Lelievre, Stacey A.,Hong, Bonnie,Brown, Josh R.,Tarkka, Richard M.,Manion, Jerald M.,Holman, Garen,Merkert, Jon W.,Vicic, David A.

, p. 9221 - 9233 (2008/10/09)

The effect of chelating phosphines was tested on the structure and pH-dependent stability of nickel-cysteine binding. (1,2-Bis(diphenylphosphino) ethane (dppe) and 1,1,1-tris[(diphenylphosphino)methyl]ethane (triphos) were used with three different cysteine derivatives (L-cysteine, Cys; L-cysteine ethyl ester, CysEt; cystamine, CysAm) to prepare complexes of the form (dppe)NiCysRn+ and (triphos)NiCysRn+ (n = 0 for Cys; n = 1 for CysEt and CysAm). Similar 31P {1H} NMR spectra for all (dppe)NiCysRn+ confirmed their square-planar P2NiSN coordination spheres. The structure of [(dppe)NiCysAm]PF6 was also confirmed by single-crystal X-ray diffraction methods. The (triphos)- NiCysAm+ and (triphos)NiCysEt+ complexes were fluxional at room temperature by 31P NMR. Upon cooling to -80°C, all gave spectra consistent with a P2NiSN coordination sphere with the third phosphorus uncoordinated. Temperature-dependent 31P NMR spectra showed that a trans P-Ni-S π interaction controlled the scrambling of the coordinated triphos. In aqueous media, (dppe)NiCys was protonated at pH ~ 4-5, leading to possible formation of a nickel-cysteinethiol and eventual cysteine loss at pH - = hydrotris(3,5-dimethylpyrazolyl)borate. Importantly, results with these heterogeneous systems demonstrated the selectivity of these nickel centers for cysteine over methionine and serine and most specifically for N-terminus cysteine. The role of Ni-S π bonding in nickel-cysteine geometries will be discussed, including how these results suggest a mechanism for the movement of electron density from nickel onto the backbone of coordinated cysteine.

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