Phosphorus-31 NMR studies of complexes of adenosine triphosphate, adenosine diphosphate, tripolyphosphate, and pyrophosphate with cobalt(III) ammines

Cornelius, Richard D.; Hart, Phillip A.; Cleland, W. W.

doi:10.1021/ic50177a025

Cited by 149 publications

(77 citation statements)

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“…Crystals of triammine(dihydrogentriphosphato)cobalt-(III), [Co(NHa)3(H2P3OI0)], were prepared as described by Cornelius, Hart & Cleland (1977). Intensity data were collected from a crystal measuring 0.07 mm x 0.15 mm x 0.17 mm on an Enraf-Nonius CAD-4 diffractometer using Ni-filtered Cu radiation (2 = 1.5418 A).…”

Section: Methodsmentioning

confidence: 99%

Structure and chelation geometry of α,β,γ-tridentate triammine(dihydrogentriphosphato)cobalt(III), [Co(NH3)3(H2P3O10)]

Merritt¹,

Sundaralingam²

1981

Acta Crystallogr Sect B

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Section: Methodsmentioning

confidence: 99%

Structure and chelation geometry of α,β,γ-tridentate triammine(dihydrogentriphosphato)cobalt(III), [Co(NH3)3(H2P3O10)]

Merritt¹,

Sundaralingam²

1981

Acta Crystallogr Sect B

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“…The product was analyzed by infrared spectroscopy (azido 2160 nm), UV-visible spectroscopy (adenine 257 nm, azidoadenine 280 nm), and fluorescence spectroscopy (dansyl residue excitation 325 nm, emission 501 nm). Synthesis of CrATP, CrAMP-PCP, and CoATP was performed by the aniline procedure of Cleland and coworkers (16,17). Co(NH 3 ) 4 PO 4 was synthesized according to Siebert (18).…”

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confidence: 99%

2′-O-Dansyl Analogs of ATP Bind with High Affinity to the Low Affinity ATP Site of Na+/K+-ATPase and Reveal the Interaction of Two ATP Sites during Catalysis

Thoenges

Schoner

1997

Journal of Biological Chemistry

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Na؉ /K ؉ -transport through mammalian cell membranes by Na ؉ /K ؉ -ATPase (EC 3.6.1.37) needs the interaction of ATP sites with different binding affinities during catalysis: one with catalytic (high affinity site) and one with regulatory properties (low affinity site). To find affinity labels for the latter one, the effects of 2-Odansylated ATP analogs on Na -ATPase binds ATP with high affinity to the sodium exporting E 1 -form (E 1 ATP binding site) and is consequently phosphorylated. After the release of sodium at the outer cell side and the following dephosphorylation, the enzyme needs a second binding of ATP. Therefore, ATP binds with low affinity to the E 2 -form (E 2 ATP binding site) of Na ϩ /K ϩ -ATPase and enhances the rate-limiting step of deocclusion of potassium during import (2, 3). In contrast to expectations deriving from this single ATP site model with its subsequent formation of the ATP sites, use of substitution-inert MgATP complex analogs has led to the postulate of a coexistence (in time and at different places) of both ATP sites (4). The Repke-Schön-Stein model (5) attempts to explain such a situation by shifting the energy excess of the sodium-transporting subunit to the potassium-transporting subunit. Each subunit follows a whole Albers-Post cycle but 180°out of phase. The bicyclic model of Plesner, on the other hand, gets its power from two ATP binding sites whose partial activities (Na ϩ -ATPase, K ϩ -phosphatase) are lower than the overall reaction (Na ϩ /K ϩ -ATPase). A single subunit does not have to pass all of the intermediates of the Albers-Post circle, but the sum fulfills all steps required for a whole turnover (6). However, there is still a lot of discussion about the intermediates shared by the partial reactions and the overall reaction (7,8).Substitution-inert MgATP complex analogs like CrATP 1 or CoATP are helpful tools to dissect the overall Na ϩ /K ϩ -ATPase activity by specific modifications of either the E 1 ATP site or the E 2 ATP site (9, 10). The activities of the E 1 ATP binding site (for example ATP/ADP exchange and "frontdoor phosphorylation") are unaffected by the inactivation of the E 2 ATP binding site by Co(NH 3 ) 4 PO 4 (11). Similarly, CrAMP-PCP, which inactivates the E 1 ATP site but is unable to phosphorylate it, does not affect activities of the E 2 ATP site, namely 86 Rb ϩ occlusion, K ϩ -activated phosphatase activity, and "backdoor phosphorylation" (12, 13). Although substitution-inert metal ATP complexes are on the one hand helpful tools to get information on basic prop-

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“…It is therefore proposed that an interaction of at least two catalytic subunits occurs during the active cation transport process by (Na' + K f )-ATPase. Preparation of cobalt tetrammine complex of ATP tetrammine ATP, C O ( N H~)~A T P , and its radioactive forms were synthesized according to Cornelius et al [33].…”

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confidence: 99%

Demonstration of cooperating alpha subunits in working (Na+ + K+)-ATPase by the use of the MgATP complex analogue cobalt tetrammine ATP

1987

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The MgATP complex analogue cobalt-tetrammine-ATP [CO(NH~)~ATP] inactivates (Na' + K ')-ATPase at Despite the inactivation of (Na' + K+)-ATPase by C O ( N H~)~A T P from the low-affinity ATP binding site, there is no change in the capacity of the high-affinity ATP binding site (Kd = 0.9 pM) nor of its capability to phosphorylate the enzyme Na+-dependently. Since (Na' + K+)-ATPase is phosphorylated Na+-dependently from the high-affinity ATP binding site although the catalytic cycle is arrested in the E2 conformational state by specific modification of the low-affinity ATP binding site, it is concluded that both ATP binding sites coexist at the same time in the working sodium pump. This demonstration of interacting catalytic subunits in the El and E2 conformational states excludes the proposal that a single catalytic subunit catalyzes (Na' + K +)-transport.Active transport of sodium and potassium through cellular membranes catalyzed by (Na' + K+)-ATPase is accompanied by conformational changes of the enzyme protein [I -41. High-and low-affinity ATP binding sites and a nonhyperbolic ATP saturation curve of the catalytic activity seem to be an expression this [5 -1 I]. While binding of ATP to the high-affinity ATP binding site appears to be essential for the Correspondence to G.

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Phosphorus-31 NMR studies of complexes of adenosine triphosphate, adenosine diphosphate, tripolyphosphate, and pyrophosphate with cobalt(III) ammines

Cited by 149 publications

References 1 publication

Structure and chelation geometry of α,β,γ-tridentate triammine(dihydrogentriphosphato)cobalt(III), [Co(NH3)3(H2P3O10)]

Structure and chelation geometry of α,β,γ-tridentate triammine(dihydrogentriphosphato)cobalt(III), [Co(NH3)3(H2P3O10)]

2′-O-Dansyl Analogs of ATP Bind with High Affinity to the Low Affinity ATP Site of Na+/K+-ATPase and Reveal the Interaction of Two ATP Sites during Catalysis

Demonstration of cooperating alpha subunits in working (Na+ + K+)-ATPase by the use of the MgATP complex analogue cobalt tetrammine ATP

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