Optimization of ATP synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium. Igamberdiev, A. U. & Kleczkowski, L. A. Front Plant Sci, 6:10, January, 2015. Edition: 2015/02/13![Optimization of ATP synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The bulk of ATP synthesis in plants is performed by ATP synthase, the main bioenergetics engine of cells, operating both in mitochondria and in chloroplasts. The reaction mechanism of ATP synthase has been studied in detail for over half a century; however, its optimal performance depends also on the steady delivery of ATP synthase substrates and the removal of its products. For mitochondrial ATP synthase, we analyze here the provision of stable conditions for (i) the supply of ADP and Mg(2+), supported by adenylate kinase (AK) equilibrium in the intermembrane space, (ii) the supply of phosphate via membrane transporter in symport with H(+), and (iii) the conditions of outflow of ATP by adenylate transporter carrying out the exchange of free adenylates. We also show that, in chloroplasts, AK equilibrates adenylates and governs Mg(2+) contents in the stroma, optimizing ATP synthase and Calvin cycle operation, and affecting the import of inorganic phosphate in exchange with triose phosphates. It is argued that chemiosmosis is not the sole component of ATP synthase performance, which also depends on AK-mediated equilibrium of adenylates and Mg(2+), adenylate transport, and phosphate release and supply.
@article{igamberdiev_optimization_2015,
title = {Optimization of {ATP} synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium},
volume = {6},
issn = {1664-462X (Print) 1664-462X (Linking)},
url = {https://www.ncbi.nlm.nih.gov/pubmed/25674099},
doi = {10.3389/fpls.2015.00010},
abstract = {The bulk of ATP synthesis in plants is performed by ATP synthase, the main bioenergetics engine of cells, operating both in mitochondria and in chloroplasts. The reaction mechanism of ATP synthase has been studied in detail for over half a century; however, its optimal performance depends also on the steady delivery of ATP synthase substrates and the removal of its products. For mitochondrial ATP synthase, we analyze here the provision of stable conditions for (i) the supply of ADP and Mg(2+), supported by adenylate kinase (AK) equilibrium in the intermembrane space, (ii) the supply of phosphate via membrane transporter in symport with H(+), and (iii) the conditions of outflow of ATP by adenylate transporter carrying out the exchange of free adenylates. We also show that, in chloroplasts, AK equilibrates adenylates and governs Mg(2+) contents in the stroma, optimizing ATP synthase and Calvin cycle operation, and affecting the import of inorganic phosphate in exchange with triose phosphates. It is argued that chemiosmosis is not the sole component of ATP synthase performance, which also depends on AK-mediated equilibrium of adenylates and Mg(2+), adenylate transport, and phosphate release and supply.},
urldate = {2021-06-07},
journal = {Front Plant Sci},
author = {Igamberdiev, A. U. and Kleczkowski, L. A.},
month = jan,
year = {2015},
note = {Edition: 2015/02/13},
keywords = {ATP synthase, adenylate kinase, chemiosmosis, chloroplasts, magnesium, mitochondria},
pages = {10},
}
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