| Range |
millions (of) 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)78841-6PubMed ID9129800
|
| 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." |
| 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) and up to 100,000 ATP molecules per second under physiological conditions (primary source, ref 13)." Please note, in primary source, VDAC channels were isolated from Neurospora crassa [red bread mold] mitochondria |
| Entered by |
Uri M |
| ID |
116550 |