Reactivity of essential thiols of myosin. Chemical probes of the activated state.

Abstract:

: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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Reisler E,Burke M,Harrington WF

doi

10.1021/bi00643a005

subject

Has Abstract

pub_date

1977-11-29 00:00:00

pages

5187-91

issue

24

eissn

0006-2960

issn

1520-4995

journal_volume

16

pub_type

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