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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
. 1980 May;77(5):2681–2683. doi: 10.1073/pnas.77.5.2681

Steady-state properties of coupled systems in mitochondrial oxidative phosphorylation.

T L Hill
PMCID: PMC349466  PMID: 6248859

Abstract

At steady state there is effective coupling among various otherwise independent membrane and internal mitochondrial systems that share the same substrates or ligands (e.g., H+, Ca2+, Pi, ADP, ATP). The number of different systems, coupled through shared substrates or ligands, is no doubt very large. But, just as an infinite series can be approximated by a finite number of terms, here the number of systems included in the analysis can be limited, as an approximation. In two previous papers, the basic but oversimplified set of four tightly coupled systems was studied. These are: respiratory chain; reverse ATPase; proton-phosphate cotransport; and ADP-ATP exchange. Essentially as illustrations of the methodology required for a more realistic analysis, two much more complicated examples are formulated here: eight tightly coupled systems, and the original four systems but with the tight coupling relaxed in two of these four.

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Selected References

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

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