| Range |
≤100000 ATP/sec
|
| Organism |
Mitochondria |
| Reference |
Choudhary OP, Paz A, Adelman JL, Colletier JP, Abramson J, Grabe M. Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1. Nat Struct Mol Biol. 2014 Jul21(7):626-32. doi: 10.1038/nsmb.2841 p.626 left column bottom paragraphPubMed ID24908397
|
| Primary Source |
[12] Rostovtseva T, Colombini M. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J. 1997 May72(5):1954-62 DOI: 10.1016/S0006-3495(97)78841-6 [13] Rostovtseva T, Colombini M. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J Biol Chem. 1996 Nov 8 271(45):28006-8PubMed ID9129800, 8910409
|
| Method |
Primary source [12] abstract: "[Investigators] measured ATP flow (using the luciferin/luciferase method) through these channels [VDAC, large aqueous pores through membranes] after reconstitution into planar phospholipid membranes." Primary source [13] abstract: "Here, direct measurements of ATP flux through VDAC channels reconstituted into planar phospholipid membranes establish that VDAC is sufficient to provide passage for ATP efflux from mitochondria." |
| Comments |
P.626 left column bottom paragraph: "In the absence of a membrane potential, VDAC1 adopts a high-conductance (450–580 pS in 100 mM KCl), anion-selective (1.7–1.9 anion-to-cation) state that is capable of passing millions of ATP molecules per second in vitro (primary source 12) and up to 100,000 ATP molecules per second under physiological conditions (primary sources)." Please note, in both primary sources, VDAC channels were isolated from Neurospora crassa [red bread mold] mitochondria |
| Entered by |
Uri M |
| ID |
116548 |