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Hypoxanthines metal complexes

Hydroxylamine, O-acetyl-N-benzoyl-N-phenyl-hydroxamic acids from, 506 Hydroxylamine ligands, 101 Hydrozirconation, 342 Hypoxanthines metal complexes, 93... [Pg.1082]

The trans isomer, on the other hand, interacts monofunctionally at the N-7 and N-1 of adenine and the N-3 of cytosine. Both isomers react monofunctionally with the N-7 of guanine and hypox-anthine. X-ray diffraction studies of the complexes formed between cis Pt(NH3)2X2 and various bases have confirmed some of the conclusions obtained from the early spectrophotometric studies. The product of the reaction between inosine and Pt(NH3)2l2 consist of two hypoxanthine rings bound to the platinum ion via the N-7 position (25). A similar structure results from the interaction of PtCl2 (en) with guanosine (26,27) again the N-7 position becomes occupied by the metal. [Pg.7]

Possibly the reason for this apparent contradiction is that the Mn +-ATP complex contains a water molecule which is simultaneously co-ordinated to the metal ion and hydrogen-bonded to N-7 of the adenine ring (see Figure 1 a similar structure has been proposed for the ATP complexes of Co + and Ni +), Thus there is an interaction between the ring and the metal ion but it is not a direct one. Further Raman work with the calcium and magnesium complexes of ATP has indicated that ATP-M-ATP interactions are more important with the larger metal than with the smaller. The relaxation spectra have been reported for the reaction of nickel(n) with 9-methylpurine, adenine, and hypoxanthine. It appears that the rate... [Pg.231]

Also, a comparison of various divalent metal cation complexes (Zn, Cu, Np ) with hypoxanthine and uracil was performed by Matsubara (Matsubara and Hirao 2002). The B3LYP level stabilization energies of both M(II)-hypoxanthine and M(II)-iu-acil complexes reflect the strength of the M-N(base) interaction, giving the same sequence Zn > Cu > Ni " " for both bases. [Pg.1283]


See other pages where Hypoxanthines metal complexes is mentioned: [Pg.135]    [Pg.3182]    [Pg.411]    [Pg.4]    [Pg.427]    [Pg.49]    [Pg.249]    [Pg.154]    [Pg.194]    [Pg.231]   
See also in sourсe #XX -- [ Pg.2 , Pg.93 ]




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