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Inactivation of myosin subfragment 1 by cobalt ii cobalt iii phenanthroline complexes 1. incorporation of cobalt iii by in situ oxidation of cobalt ii



Inactivation of myosin subfragment 1 by cobalt ii cobalt iii phenanthroline complexes 1. incorporation of cobalt iii by in situ oxidation of cobalt ii



Biochemistry 18(22): 4793-4799



Rabbit myosin's chymotrypic subfragment 1 (SF1) ATPase activity is rapidly inactivated in a mixture containing CoCl2, 1,10-phenanthroline (phen), and [CoIII(phen)2CO3]+. The inactivation results from the incorporation of exchange-inert Co(III). The inactivation can be quenched but not reversed by addition of EDTA in quantities stoichiometric with Co2+ and can be completely reversed by addition of a variety of reducing agents such as NaBH4, FeIIEDTA, cobaltous cyanide or [Co(phen)3]2+ which allow removal of cobalt(III) and restoration of ATPase activity. 57Co(II) labeling studies indicate that greater than 93% of the cobalt incorporated into SF1 is incorporated via a Co(II) intermediate. A mechanism may exist whereby an exchange-labile CoII(phen)x complex is rapidly and reversibly chelated by SF1. The CoII(phen)x.cntdot.enzyme complex is oxidized in situ by [CoIII(phen)2CO3]+ to yield an exchange-inert CoIII(phen)x.cntdot.SF1 complex with no ATPase activity. Inactivations of SF1 which result from CoII(phen)x in situ oxidation by either H2O2 or O2 are not reversed by reducing agents, despite the removal of bound Co. In situ oxidation of CoII(phen)x by the single electron-accepting oxidant [CoIII(phen)2CO3]+ may result in a very mild incorporation of Co(III) into SF1. This approach may have general application for the incorporation of Co(III) into proteins.

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