Quantum coherent contributions in biological electron transfer

Details Quantum coherent contributions in biological electron transfer Quantum coherent contributions in biological electron transfer

2011-11-07

arxiv.org/abs/1111.1646v2

Biology

Quantitative Biology

Biomolecules

Scientific paper

Many biological electron transfer (ET) reactions are mediated by metal centres in proteins. NADH:ubiquinone oxidoreductase (complex I) contains an intramolecular chain of seven iron-sulphur (FeS) clusters, one of the longest chains of metal centres in biology and a test case for physical models of intramolecular ET. In biology, intramolecular ET is commonly described as a diffusive hopping process, according to the semi-classical theories of Marcus and Hopfield. However, recent studies have raised the possibility that non-trivial quantum mechanical effects play a functioning role in certain biomolecular processes. Here, we extend the semi-classical model for biological ET to incorporate both semi-classical and coherent quantum phenomena using a quantum master equation based on the Holstein Hamiltonian. We test our model on the structurally-defined chain of FeS clusters in complex I. By exploring a wide range of realistic parameters we find that, when the energy profile for ET along the chain is relatively flat, just a small coherent contribution can provide a robust and significant increase in ET rate (above the semi-classical diffusive-hopping rate), even at physiologically-relevant temperatures. Conversely, when the on-site energies vary significantly along the chain the coherent contribution is negligible. For complex I, a crucial respiratory enzyme that is linked to many neuromuscular and degenerative diseases, our results suggest a new contribution towards ensuring that intramolecular ET does not limit the rate of catalysis. For the emerging field of quantum biology, our model is intended as a basis for elucidating the general role of coherent ET in biological ET reactions.

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