Abstract
Magnetic interactions within Mn-(μ-O)2-Mn pairs are crucial to the function of some essential enzymes and catalysts, but their nature is unclear. Neutron diffraction reveals that similar units in BiMnPO5 show ferromagnetic coupling which has been rationalized by density functional theory modelling and calculations of magnetic exchange energies. The results are important to many solid state and biological systems.
Highlights
Magnetic interactions within Mn–(l-O)2–Mn pairs are crucial to the function of some essential enzymes and catalysts, but their nature is unclear
Neutron diffraction reveals that similar units in BiMnPO5 show ferromagnetic coupling which has been rationalized by density functional theory modelling and calculations of magnetic exchange energies
The results are important to many solid state and biological systems
Summary
Magnetic interactions within Mn–(l-O)2–Mn pairs are crucial to the function of some essential enzymes and catalysts, but their nature is unclear. Simple Mn–(m-O)2–Mn pairs are found in enzymes (e.g. arginase, catalase, and Ribonucleotide Reductase (RNR)), which are found in most living organisms including humans.[7] Various studies on these and their biomimetic counterparts have greatly enhanced our understanding of their structure and function.[8] Magnetically, binuclear Mn(II, II) pairs generally show AFM coupling to give an S = 0 unit, but some synthetic analogues with various ligands show FM behaviour.[9] Complementary experimental and theoretical studies have probed the exchange mechanisms within the pairs but no reliable roadmap exists to allow reliable predictions.9h
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