Reactivity of essential thiols of myosin. Chemical probes of the activated state.
14C-Labeled fluorodinitrobenzene and N-ethylmaleimide have been used as chemical probes of the conformational states of myosin induced by the binding of MgADP and MgATP. The results indicate that in the high-energy conformation, MMgADP-Pi, the essential thiols are protected from modification but their diminished reactivity does not result from depletion of the reagent by reaction at nonessential thiols. The binding of MgADP to myosin exposes the essential thiols as reflected by an increased rate of their modification. The influence of the divalent cations Mg2+ and Ca2+ on the conformation of the M species has also been investigated. By monitoring the incorporation of fluorodinitrobenzene, the conformations of the M state in the presence of these cations can be clearly discerned.
D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate; D001665:Binding Sites; D004139:Dinitrofluorobenzene; D004492:Edetic Acid; D005033:Ethylmaleimide; D007700:Kinetics; D008274:Magnesium; D009218:Myosins / Q000378:metabolism; D013438:Sulfhydryl Compounds
D013438:Sulfhydryl Compounds; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D004139:Dinitrofluorobenzene; D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium; D005033:Ethylmaleimide