Direct observation using an ultra-high-speed optical trap revealed that the working stroke of β-cardiac myosin can occur within <200 μs of actin binding and precedes phosphate release.
Direct observation of single-molecule cardiac myosin mechanics reveals that the force-generating working stroke occurs within <200 μs of actin binding and precedes phosphate release.
Key steps of cardiac mechanochemistry, including the force-generating working stroke and the release of phosphate (Pi), occur rapidly after myosin-actin attachment. An ultra-high-speed optical trap enabled direct observation of the timing and amplitude of the working stroke, which can occur within <200 μs of actin binding by β-cardiac myosin. The initial actomyosin state can sustain loads of at least 4.5 pN and proceeds directly to the stroke or detaches before releasing ATP hydrolysis products. The rates of these processes depend on the force. The time between binding and stroke is unaffected by 10 mM Pi which, along with other findings, indicates the stroke precedes phosphate release. After Pi release, Pi can rebind enabling reversal of the working stroke. Detecting these rapid events under physiological loads provides definitive indication of the dynamics by which actomyosin converts biochemical energy into mechanical work.
Woody et al. (Tue,) reported a other. Ultra-high-speed optical trap was evaluated on Timing and amplitude of the working stroke of β-cardiac myosin. Direct observation using an ultra-high-speed optical trap revealed that the working stroke of β-cardiac myosin can occur within <200 μs of actin binding and precedes phosphate release.
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