26th Australian Institute of Physics Congress and the Australian and New Zealand Conference on Optics and Photonics

A mechanistic analysis of magnetic field effects in ATP synthesis

7 Dec 2026, 16:30

15m

Belinda Hutchinson Building (The University of Sydney )

Contributed Oral AIP | Atomic and Molecular Physics (ATMOP) AIP ATMOP: Collisions, Molecules, Chemical Physics

Speaker

Anjay Manian (The University of Wollongong)

Description

Magnetic field effects (MFEs) and magnetic isotope effects (MIEs) have been proposed as potential modulator of adenosine triphosphate (ATP) synthesis via a transient spin dependent intermediate due to coupling between adenosine diphosphate (ADP) and a free ion. The hypothesis originally advanced by Buchachenko et al.[1] has motivated significant theoretical and experimental interest; however, independent confirmation of these phenomena is limited and is a subject of ongoing debate[2,3]. Here, we investigate the microscopic conditions under which magnetic sensitivity may emerge in spin-sensitive chemistry in the ATP synthesis model[4]. Using a quantum dynamical framework motivated by phonon-assisted quantum chemistry, we examine the role of spin-orbit-mediated and hyperfine-mediated spin mixing. Our results indicate that phonon-mediated contributions dominate spin evolution under biologically relevant parameter regimes, leading to field-dependent modulation of spin populations. In particular, we identify regimes of orientation-independent (5 mT) and orientation-dependent (50 mT) field strengths which facilitate enhanced spin evolution. This does not result in any significant MFE, but a clear MIE is observed when incorporating vibronic contributions, increasing ATP synthesis yields by up to 45% with respect to downstream radical pair population kinetics. These findings define microscopic constraints under which magnetic sensitivity may arise in ATP synthesis and provide a mechanistic framework that refines the previously proposed model, offering testable signatures of magnetosensitvity in enzymatic systems.

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[1] Buchachenko, Kuznetsov, & Arkhangel’sky; Doklady Biochemistry
and Biophysics, 2004; 396, 1-6, 197–199.
[2] Crotty, Silkstone, Poddar, Ranson, Prina-Mello, Wilson, & Coey;
Proceedings of the National Academy of Sciences, 2011; 109, 5,
1437-1442.
[3] Hore; Proceedings of the National Academy of Sciences, 2012; 109, 5,
1357–1358.
[4] Manian, Paz, Raza, & Yu; ChemRXIV:10.26434/chemrxiv.15000458/v1.