ATP合酶
线粒体
化学渗透
生物能学
生物
生物化学
电子传输链
ATP-ADP转位酶
生物物理学
细胞质
酶
线粒体内膜
作者
Peyman Fahimi,Chérif F. Matta
出处
期刊:Physical Biology
[IOP Publishing]
日期:2021-04-14
卷期号:18 (4): 04LT01-04LT01
被引量:8
标识
DOI:10.1088/1478-3975/abf7d9
摘要
Abstract Recent experiments and thermodynamic arguments suggest that mitochondrial temperatures are higher than those of the cytoplasm. A “hot mitochondrion” calls for a closer examination of the energy balance that endows it with these claimed elevated temperatures. As a first step in this effort, we present here a semi-quantitative bookkeeping whereby, in one stroke, a formula is proposed that yields the rate of heat production in a typical mitochondrion and a formula for estimating the number of “ active ” ATP synthase molecules per mitochondrion. The number of active ATP synthase molecules is the equivalent number of ATP synthases operating at 100% capacity to maintain the rate of mitochondrial heat generation. Scaling laws are shown to determine the number of active ATP synthase molecules in a mitochondrion and mitochondrial rate of heat production, whereby both appear to scale with cell volume. Four heterotrophic protozoan cell types are considered in this study. The studied cells, selected to cover a wide range of sizes (volumes) from ca. 100 μ m 3 to 1 million μ m 3 , are estimated to exhibit a power per mitochondrion ranging from ca. 1 pW to 0.03 pW. In these cells, the corresponding number of active ATP synthases per mitochondrion ranges from 5000 to just about a hundred. The absolute total number of ATP synthase molecules per mitochondrion, regardless of their activity status, can be up to two orders of magnitudes higher.
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