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Identification of the transitory complex myosin-ATP by the use of α,β-methylene-ATP

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Mannherz,  Hans Georg
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Barrington Leigh,  J.
Max Planck Institute for Medical Research, Max Planck Society;

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Holmes,  Kenneth C.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Rosenbaum,  G.
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Mannherz, H. G., Barrington Leigh, J., Holmes, K. C., & Rosenbaum, G. (1973). Identification of the transitory complex myosin-ATP by the use of α,β-methylene-ATP. Nature, 241, 226-229. doi:10.1038/newbio241226a0.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-901B-0
Abstract
FROM structural studies on glycerinated Lethocerus flight muscle Ready, Holmes and Tregear1 showed that the cross-bridges of insect flight muscle take on recognizably different configurations in the presence and absence of ATP. In the presence of excess ATP (relaxed) the bridges are approximately at right-angles to the myosin thick filament and in its absence (rigor state, with formation of the actomyosin complex) they make a chevron-like structure by binding at an angle of about 45° to the actin filaments. Coupled with studies on living frog muscle2 this led to proposals by Huxley3 and Pringle4 that the cross-bridges move the actin filament past the myosin filament by a kind of rowing action; a model which has been generally accepted as a working hypothesis.