期刊
ELIFE
卷 8, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.49266
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资金
- National Institutes of Health [P01-GM087253, R01-HL133863, R35-GM118139]
- National Science Foundation NSF GRFP
- Ente Cassa di Risparmio di Firenze Marco Capitanio
- Horizon 2020 Framework Programme [654148]
- National Science Foundation [CMMI: 15-48571]
Key steps of cardiac mechanochemistry, including the force-generating working stroke and the release of phosphate (P-i), 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 mu s of actin binding by beta-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 P-i which, along with other findings, indicates the stroke precedes phosphate release. After P-i release, P-i 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.
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