I would like to expand on the structure  and  function of ATP synthase’s domains and subunits. Subunits have their own function that help for example, in  F1 which is water soluble plays a major role in hydrolysis which was not stated in the article.  I would also like to expand on the ATP synthase regulation and conformational change. Any feedback or suggestions would be greatly appreciated. Thank you.

[1]https://app.perusall.com/courses/chemistry-153a-spring-2017

  1. ^ Esparza-Moltó, Pau B.; Nuevo-Tapioles, Cristina; Cuezva, José M. (2017-02-06). "Regulation of the H(+)-ATP synthase by IF1: a role in mitohormesis". Cellular and molecular life sciences: CMLS. doi:10.1007/s00018-017-2462-8. ISSN 1420-9071. PMID 28168445.

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  1. ^ Esparza-Moltó, Pau B.; Nuevo-Tapioles, Cristina; Cuezva, José M. (2017-02-06). "Regulation of the H(+)-ATP synthase by IF1: a role in mitohormesis". Cellular and molecular life sciences: CMLS. doi:10.1007/s00018-017-2462-8. ISSN 1420-9071. PMID 28168445.
  2. ^ Nakanishi-Matsui, Mayumi; Sekiya, Mizuki; Futai, Masamitsu (2016-02-01). "ATP synthase from Escherichia coli: Mechanism of rotational catalysis, and inhibition with the ε subunit and phytopolyphenols". Biochimica Et Biophysica Acta. 1857 (2): 129–140. doi:10.1016/j.bbabio.2015.11.005. ISSN 0006-3002. PMID 26589785.
  3. ^ Maierean, Serban; Serban, Maria-Corina; Rizzo, Manfredi; Lippi, Giuseppe; Sahebkar, Amirhossein; Banach, Maciej (2017-02-07). "The potential role of mitochondrial ATP synthase inhibitory factor 1 (IF1) in coronary heart disease: a literature review". Lipids in Health and Disease. 16 (1): 35. doi:10.1186/s12944-017-0430-9. ISSN 1476-511X. PMC 5297070. PMID 28173810.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  4. ^ Nath, Sunil (2017-05-01). "Analysis of molecular mechanisms of ATP synthesis from the standpoint of the principle of electrical neutrality". Biophysical Chemistry. 224: 49–58. doi:10.1016/j.bpc.2017.03.002. ISSN 1873-4200. PMID 28318906.