Abstract
The formation constants of the complexes of adenyl-5'-yl imidodiphosphate with H+ Mg2+, Ca2+ and a number of bivalent transition-metal ions were measured potentionmetrically. The complexes are generally a little more stable than the analogous complexes of ATP. By measuring the formation constants at two temperatures, this increase in stability was shown to result from an increased enthalpy change on complex-formation.
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Selected References
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- Eady R. R., Kennedy C., Smith B. E., Thorneley R. N., Yates G., Postgate J. R. Nitrogenase in Azotobacter chroococcum and Klebsiella pneumoniae. Biochem Soc Trans. 1975;3(4):488–492. doi: 10.1042/bst0030488. [DOI] [PubMed] [Google Scholar]
- Mohan M. S., Rechnitz G. A. Ion-electrode study of the calcium-adenosine triphosphate system. J Am Chem Soc. 1972 Mar 8;94(5):1714–1716. doi: 10.1021/ja00760a048. [DOI] [PubMed] [Google Scholar]
- Phillips R. C., George P., Rutman R. J. Thermodynamic studies of the formation and ionization of the magnesium(II) complexes of ADP and ATP over the pH range 5 to 9. J Am Chem Soc. 1966 Jun 20;88(12):2631–2640. doi: 10.1021/ja00964a002. [DOI] [PubMed] [Google Scholar]
- Philo R. D., Selwyn M. J. Inhibition of the soluble adenosine triphosphatase from mitochondria by adenylyl imidodiphosphate. Biochem J. 1974 Dec;143(3):745–749. doi: 10.1042/bj1430745. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yount R. G., Babcock D., Ballantyne W., Ojala D. Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P--N--P linkage. Biochemistry. 1971 Jun 22;10(13):2484–2489. doi: 10.1021/bi00789a009. [DOI] [PubMed] [Google Scholar]
- Yount R. G., Ojala D., Babcock D. Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosin. Biochemistry. 1971 Jun 22;10(13):2490–2496. doi: 10.1021/bi00789a010. [DOI] [PubMed] [Google Scholar]
