Potentiometric determination of the stability constants of a model (Na + K)ATPase complex |
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| Authors: | Graham E. Jackson Mark J. Kelly |
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| Affiliation: | Department of Inorganic Chemistry, University of Cape Town, Rondebosch 7700, South Africa |
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| Abstract: | Formation constants for the binary and ternary Mn(II)-nitrilotriacetic acid (NTA) and adenosine triphosphate (ATP) which model the action of (Na+ + K+) ATPase have been determined at 25°C and I = 150 mmole dm-3 NaCl. The results are interpreted in terms of the known stabilities of the enzyme complexes and it is concluded that metal-ion chelation of ATP alone is not enough for hydrolysis to occur. A substantial stabilisation of the ternary complex occurs, possibly through bridging sodium ions. |
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| Keywords: | Author to whom correspondence should be addressed. |
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