OxPhos Revisited: A Five-Dimensional Comparative Analysis of Chemiosmosis and Conformons

Sungchul Ji, Ph.D.
Emeritus Professor of Theoretical Cell Biology
Rutgers University
Piscataway, New Jersey

1. Introduction: Beyond the Proton Gradient

For over six decades, Peter Mitchell’s chemiosmotic model of oxidative phosphorylation (OxPhos) [1, 2] has dominated bioenergetics. It offered a simple yet revolutionary view: electron transport generates a proton gradient (PMF), and this gradient powers ATP synthesis. But does this elegant model tell the whole story?

A growing body of evidence—mechanistic, quantum, and enzymological—suggests otherwise. The conformon model, co-developed by D.E. Green and myself in the early 1970s [3, 4], proposes that oxidative phosphorylation involves more than passive proton diffusion. It introduces conformons [5, 6]—quantized packets of mechanical energy and information—as the dynamic intermediates that couple respiration to ATP formation [7].

To clarify the relationship between these two frameworks, I present here a five-dimensional Venn-type comparative analysis (5VCA) recently developed in [8], distinguishing their commonalities, differences, and complementarities.

2. Diagrammatic Summary (Text Description)

Imagine two overlapping circles:

• Circle A: Chemiosmotic Model (CM)

• Circle B: Conformon Model (CoM)

The overlapping region includes:

• Proton-driven ATP synthesis

• ETC and ATP synthase as core machinery

• Proton pumping as an essential function

The non-overlapping area of CM: D(A)

• Bulk diffusion model

• No mechanical intermediates

• No quantum considerations

The non-overlapping area of CoM: D(B)

• Conformons

• Localized coupling and proton wires

• Quantum mechanical and informational aspects

• Generalized Franck-Condon Principle
  The complementary space: C(C)

• PMF is understood as a macro-effect

• Conformons act as micro-mechanical causes

• Chemiosmosis emerges from conformon-mediated dynamics

3. Conclusion: From Phenomenon to Mechanism

The chemiosmotic model gave us a phenomenological map: it pointed to what happens in OxPhos. The conformon model attempts to explain how it happens—by tracing the causal pathway from electron transfer through conformational changes to ATP synthesis.

As such, the conformon model may be viewed as not a rejection of chemiosmosis, but as its mechanistic and quantum-mechanical completion.

To borrow a metaphor: "The chemiosmotic model is to the conformon model what astrology is to astronomy."

Both gaze at the stars. But only one asks: what forces shaped them?

References:
[1] Mitchell, P. (1961). Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature 191:144-148.
[2] Mitchell, P. (1966). Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 41: 445-502.
[3] Green, D. E. and Ji, S. (1972). The Electromechanochemical Model of Mitochondrial Structure and Function, in: Molecular Basis of Electron Transport (Schulz, J. and Cameron, B. F., eds.), Academic Press, New York, pp. 1-44.
[4] Ji, S. (1976). A Model of Oxidative Phosphorylation that Accommodates the Chemical Intermediate, Chemiosmotic, Localized Proton, and Conformational Hypotheses. J. theoret. Biol. 59, 319-330.
[5] Ji, S. (2000). Free energy and Information Contents of Conformons in proteins and DNA, BioSystems 54, 107-130.
[6] Conformons. https://en.wikipedia.org/wiki/Conformon
[7] Ji, S. (2025). Chemiosmotic vs Conformon Models of Oxidative Phosphorylation: Theory and Mechanistic Insights. BioSytems (in press).
[8] Ji, S. (2025). Bridging Global Conflicts and Inner Peace: Toward a Semiotic–Spiritual Synthesis. https://622622.substack.com/p/bridging-global-conflicts-and-inner