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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Jul;76(7):3203–3207. doi: 10.1073/pnas.76.7.3203

Theoretical methods for study of kinetics of models of the mitochondrial respiratory chain.

T L Hill, T R Chay
PMCID: PMC383792  PMID: 226961

Abstract

In earlier work, Hill and Chance obtained exact steady-state kinetic properties for partial models of the mitochondrial respiratory chain with two isopotential pools and one four-state "site enzyme" between the two pools. That work is extended here to full models of the respiratory chain with four isopotential pools and three four-state site enzymes between pairs of pools. Because of the complexity of the model, exact calculations are no longer possible. Instead, we show, by means of some examples, the feasibility of using Monte Carlo calculations on all cases and numerical solution of thousands of kinetic differential equations in many cases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alexandre A., Reynafarje B., Lehninger A. L. Stoichiometry of vectorial H+ movements coupled to electron transport and to ATP synthesis in mitochondria. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5296–5300. doi: 10.1073/pnas.75.11.5296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chance B. Electron transfer: pathways, mechanisms, and controls. Annu Rev Biochem. 1977;46:967–980. doi: 10.1146/annurev.bi.46.070177.004535. [DOI] [PubMed] [Google Scholar]
  3. DeVault D. Theory of iron-sulfur center N-2 oxidation and reduction by ATP. J Theor Biol. 1976 Oct 7;62(1):115–139. doi: 10.1016/0022-5193(76)90054-0. [DOI] [PubMed] [Google Scholar]
  4. Devault D. Energy transduction in electron transport. Biochim Biophys Acta. 1971 Jan 12;226(1):193–199. doi: 10.1016/0005-2728(71)90192-7. [DOI] [PubMed] [Google Scholar]
  5. Hill T. L., Chance B. Steady-state kinetics of models of respiratory chain enzymes with isopotential pools and conformational site enzymes. J Theor Biol. 1978 May 8;72(1):17–56. doi: 10.1016/0022-5193(78)90016-4. [DOI] [PubMed] [Google Scholar]
  6. Hill T. L. Coupled enzyme systems in a vesicular membrane: oxidative phosphorylation as an example. Proc Natl Acad Sci U S A. 1979 Jan;76(1):232–235. doi: 10.1073/pnas.76.1.232. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hill T. L. Steady-state coupling of four membrane systems in mitochondrial oxidative phosphorylation. Proc Natl Acad Sci U S A. 1979 May;76(5):2236–2238. doi: 10.1073/pnas.76.5.2236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Nicholls D. G. The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution. Eur J Biochem. 1974 Dec 16;50(1):305–315. doi: 10.1111/j.1432-1033.1974.tb03899.x. [DOI] [PubMed] [Google Scholar]
  9. Rottenberg H. The measurement of transmembrane electrochemical proton gradients. J Bioenerg. 1975 May;7(2):61–74. doi: 10.1007/BF01558427. [DOI] [PubMed] [Google Scholar]

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