The Complex Roles of Adenosine Triphosphate in Bioenergetics.
ABS transporters
hydrolysis
ionic pumps
phosphorylation
“high energy” bonds
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
18 05 2022
18 05 2022
Historique:
revised:
16
03
2022
received:
29
01
2022
pubmed:
31
3
2022
medline:
21
5
2022
entrez:
30
3
2022
Statut:
ppublish
Résumé
ATP is generally defined as the "energy currency" of the cell. Its phosphoanhydride P-O bonds are often considered to be "high energy" linkages that release free energy when broken, and its hydrolysis is described as "strongly exergonic". However, breaking bonds cannot release energy and ATP hydrolysis in motor and active transport proteins is not "strongly exergonic". So, the relevance of ATP resides elsewhere. As important as the nucleotide are the proteins that undergo functionally relevant conformational changes upon both ATP binding and release of ADP and inorganic phosphate. ATP phosphorylates proteins for signaling, active transport, and substrates in condensation reactions. The ensuing dephosphorylation has different consequences in each case. In signaling and active transport the phosphate group is hydrolyzed whereas in condensation reactions the phosphoryl fragment acts as a dehydrating agent. As it will be discussed in this article, ATP does much more than simply contribute free energy to biological processes.
Identifiants
pubmed: 35353443
doi: 10.1002/cbic.202200064
doi:
Substances chimiques
Phosphates
0
Adenosine Diphosphate
61D2G4IYVH
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202200064Informations de copyright
© 2022 Wiley-VCH GmbH.
Références
F. Lipmann, in Advances in Enzymology: and Related Areas of Molecular Biology (Eds.: F. F. Nord, C. H. Werkman), Wiley, Hoboken, 2006, pp. 99-162.
E. A. Ruben, J. A. Plumley, M. S. Chapman, J. D. Evanseck, J. Am. Chem. Soc. 2008, 130, 3349-3358.
P. George, R. J. Witonsky, M. Trachtman, C. Wu, W. Dorwart, L. Richman, W. Richman, F. Shurayh, B. Lentz, Biochim. Biophys. Acta 1970, 223, 1-15.
P. V. Attwood, P. G. Besant, M. J. Piggott, Amino Acids 2011, 40, 1035-1051.
M. M. Cooper, M. W. Klymkowsky, CBE Life Sci. Educ. 2013, 12, 306-312.
F. A. Kiani, S. Fischer, Phys. Chem. Chem. Phys. 2016, 18, 20219-20233.
M. Prieß, H. Göddeke, G. Groenhof, L. V. Schäfer, ACS Cent. Sci. 2018, 4, 1334-1343.
B. W. Dreyfus, B. D. Geller, V. Sawtelle, J. Svoboda, C. Turpen, E. F. Redish, 2012 Physics Education Research Conference, AIP Conf. Proc. 2013, 1513, 122-125.
J. D. Christian, J. Chem. Educ. 1973, 50, 176-177.
J. M. Berg, J. L. Tymoczko, L. Stryer, Biochemistry, 5th ed., 2002.
Nelson D. L., M. M. Cox, Lehninger Principles of Biochemistry, W. H. Freeman and Company, New York, 2004.
L. Demeis, Arch. Biochem. Biophys. 1993, 306, 287-296.
C. R. Bagshaw, D. R. Trentham, Biochem. J. 1973, 133, 323-328.
A. E. Senior, S. Nadanaciva, J. Weber, Biochim. Biophys. Acta Bioenerg. 2002, 1553, 188-211.
K. Favazzo, M. Sendzik, D. Feigl, “Glutamine Synthetase,” (accessed 19/04/2021) https://chem.libretexts.org/@go/page/98114, 2019.
M. Dittrich, S. Hayashi, K. Schulten, Biophys. J. 2003, 85, 2253-2266.
G. Grüber, H. Wieczorek, W. R. Harvey, V. Müller, J. Exp. Biol. 2001, 204, 2597-2605.
J. E. Walker, Biochem. Soc. Trans. 2013, 41, 1-16.
S. Hayashi, H. Ueno, A. R. Shaikh, M. Umemura, M. Kamiya, Y. Ito, M. Ikeguchi, Y. Komoriya, R. Iino, H. Noji, J. Am. Chem. Soc. 2012, 134, 8447-8454.
Y. Q. Gao, W. Yang, M. Karplus, Cell 2005, 123, 195-205.
A. Houdusse, H. L. Sweeney, Trends Biochem. Sci. 2016, 41, 989-997.
T. Kawakubo, O. Okada, T. Minami, Biophys. Chem. 2005, 115, 77-85.
T. Kawakubo, O. Okada, T. Minami, Biophys. Chem. 2009, 141, 75-86.
M. McCullagh, M. G. Saunders, G. A. Voth, J. Am. Chem. Soc. 2014, 136, 13053-13058.
M. J. Kushmerick, R. E. Davies, Proc. R. Soc. London Ser. B 1969, 174, 315-353.
R. W. Hanson, Bioch. Educ. 1989, 17, 86-92.
W. Hwang, M. Karplus, Proc. Natl. Acad. Sci. USA 2019, 116, 19777-19785.
S. Wilkens, F1000Prime Rep 2015, 7, https://doi.org/10.12703/P7-14.
C. F. Higgins, Res. Microbiol. 2001, 152, 205-210.
J. Dong, G. Yang, H. S. McHaourab, Science 2005, 308, 1023-1028.
P. Zou, H. S. McHaourab, J. Mol. Biol. 2009, 393, 574-585.
T. Hayashi, S. Chiba, Y. Kaneta, T. Furuta, M. Sakurai, J. Phys. Chem. B 2014, 118, 12612-12620.
S. Mishra, B. Verhalen, R. A. Stein, P.-C. Wen, E. Tajkhorshid, H. S. Mchaourab, eLife 2014, 3, e02740.
H. Göddeke, M. H. Timachi, C. A. J. Hutter, L. Galazzo, M. A. Seeger, M. Karttunen, E. Bordignon, L. V. Schäfer, J. Am. Chem. Soc. 2018, 140, 4543-4551.
H. Göddeke, L. V. Schäfer, J. Am. Chem. Soc. 2020, 142, 12791-12801.
G. Lu, J. M. Westbrooks, A. L. Davidson, J. Chen, Proc. Natl. Acad. Sci. USA 2005, 102, 17969-17974.
T. Hayashi, S. Chiba, Y. Kaneta, T. Furuta, M. Sakurai, J. Phys. Chem. B 2014, 118, 12612-12620.
B. Gamoke, D. Neff, J. Simons, J. Phys. Chem. A 2009, 113, 5677-5684.
Y. Shi, Cell 2009, 139, 468-484.
Z. Wang, P. A. Cole, Meth. Enzymol. 2014, 548, 1-21.
F. Ardito, M. Giuliani, D. Perrone, G. Troiano, L. L. Muzio, Int. J. Mol. Med. 2017, 40, 271-280.
M. Valiev, J. Yang, J. A. Adams, S. S. Taylor, J. H. Weare, J. Phys. Chem. B 2007, 111, 13455-13464.
P. L. Jørgensen, J. P. Andersen, J. Membr. Biol. 1988, 103, 95-120.
P. L. Jorgensen, K. O. Hakansson, S. J. D. Karlish, Annu. Rev. Physiol. 2003, 65, 817-849.
A.-M. L. Jensen, T. L.-M. Sørensen, C. Olesen, J. V. Møller, P. Nissen, EMBO J. 2006, 25, 2305-2314.
S.-H. Liaw, I. Kuo, D. Eisenberg, Protein Sci. 1995, 4, 2358-2365.
G. Di Sabato, W. P. Jencks, J. Am. Chem. Soc. 1961, 83, 4393-4400.
C.-Y. Chou, L. P. C. Yu, L. Tong, J. Biol. Chem. 2009, 284, 11690-11697.
X. C. Zhang, H. Zhang, Biophys. Rep. 2019, 5, 167-175.
W. P. Jencks, in Methods in Enzymology, Elsevier, Amsterdam, 1989, 171, pp. 145-164.
A. H. Klein, A. Shulla, S. A. Reimann, D. H. Keating, A. J. Wolfe, J. Bacteriol. 2007, 189, 5574-5581.
G. Di Sabato, W. P. Jencks, J. Am. Chem. Soc. 1961, 83, 4400-4405.
A. J. Kirby, F. Nome, Acc. Chem. Res. 2015, 48, 1806-1814.
M. J. Kushmerick, R. E. Larson, R. E. Davies, Proc. R. Soc. London Ser. B 1969, 174, 293-313.
K. D. Wilkinson, I. A. Rose, J. Biol. Chem. 1979, 254, 12567-12572.
D. K. Srivastava, S. A. Bernhard, Annu. Rev. Biophys. Biophys. Chem. 1987, 16, 175-204.
X. C. Zhang, W. Feng, Biophys. Rep. 2016, 2, 87-94.
O. Miyashita, P. G. Wolynes, J. N. Onuchic, J. Phys. Chem. B 2005, 109, 1959-1969.
N. Tokuriki, D. S. Tawfik, Science 2009, 324, 203-207.
S. Lu, W. Huang, Q. Wang, Q. Shen, S. Li, R. Nussinov, J. Zhang, PLoS Comp. Biol. 2014, 10, e1003831.
D. H. Williams, E. Stephens, D. P. O'Brien, M. Zhou, Angew. Chem. Int. Ed. 2004, 43, 6596-6616;
Angew. Chem. 2004, 116, 6760-6782.
J. F. Brandts, C. Q. Hu, L. N. Lin, M. T. Mas, Biochemistry 1989, 28, 8588-8596.
Y. Fukushima, M. Ushimaru, Proc. Jpn. Acad. Ser. B 2001, 77, 68-72.
A. Kirschning, Angew. Chem. Int. Ed. 2021, 60, 6242-6269;
Angew. Chem. 2021, 133, 6308-6337.
B. Damer, D. Deamer, Life 2015, 5, 872-887.
H. M. Fares, A. E. Marras, J. M. Ting, M. V. Tirrell, C. D. Keating, Nat. Commun. 2020, 11, 5423.
J. C. Fontecilla-Camps, J. Inorg. Biochem. 2021, 216, 111347.
J. Dunn, M. H. Grider, Physiology, Adenosine Triphosphate in StatPearls [internet], StatPearls Publishing, Treasure Island (FL), 2021, Bookshelf ID: NBK553175.