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A reversible temperature-dependent high-spin to low-spin transition with T  1/2 = -60 °C has been observed in the resonance Raman spectra of the equilibrium reduced and photoreduced heme a  3 of the thermophilic ba  3 heme-copper oxidoreductase. The transition is based on the frequency shifts of the spin-state marker bands ν  2 (C b C b ) and ν  10 (C a C m ) and is attributed to the displacement of the heme iron along the heme normal as a consequence of the Fe-Np repulsion at temperature below -40 °C which will increase the ligand field strength forcing the pairing of d electrons into the lower energy orbitals.

Reversible temperature-dependent high- to low-spin transition in the heme Fe–Cu binuclear center of cytochrome ba3 oxidase

Reversible temperature-dependent high- to low-spin transition in the heme Fe–Cu binuclear center of cytochrome ba₃ oxidase