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• W2078454267 abstract "Magnesium (Mg2+) is the physiological divalent cation stabilizing nucleotide or nucleotide analog in the active site of myosin subfragment 1 (S1). In the presence of fluoride, Mg2+ and MgADP form a complex that traps the active site of S1 and inhibits myosin ATPase. The ATPase inactivation rate of the magnesium trapped S1 is comparable but smaller than the other known γ-phosphate analogs at 1.2 M−1 s−1 with 1 mM MgCl2. The observed molar ratio of Mg/S1 in this complex of 1.58 suggests that magnesium occupies the γ-phosphate position in the ATP binding site of S1 (S1–MgADP–MgFx). The stability of S1–MgADP–MgFx at 4°C was studied by EDTA chase experiments but decomposition was not observed. However, removal of excess fluoride causes full recovery of the K+-EDTA ATPase activity indicating that free fluoride is necessary for maintaining a stable trap and suggesting that the magnesium fluoride complex is bonded to the bridging oxygen of β-phosphate more loosely than the other known phosphate analogs. The structure of S1 in S1–MgADP–MgFx was studied with near ultraviolet circular dichroism, total tryptophan fluorescence, and tryptophan residue 510 quenching measurements. These data suggest that S1–MgADP–MgFx resembles the M**·ADP·Pi steady-state intermediate of myosin ATPase. Gallium fluoride was found to compete with MgFx for the γ-phosphate site in S1–MgADP–MgFx. The ionic radius and coordination geometry of magnesium, gallium and other known γ-phosphate analogs were compared and identified as important in determining which myosin ATPase intermediate the analog mimics." @default.
• W2078454267 created "2016-06-24" @default.
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• W2078454267 creator A5022370263 @default.
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• W2078454267 date "1999-02-01" @default.
• W2078454267 modified "2023-10-17" @default.
• W2078454267 title "Inhibition of myosin ATPase by metal fluoride complexes" @default.
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• W2078454267 doi "https://doi.org/10.1016/s0167-4838(98)00262-3" @default.
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