Weakly bound complexes between ferric heme cations and NO were synthesised in the gas phase from ion–molecule reactions, and their absorption measured based on photodissociation yields. The Soret band, which serves as an important marker band for heme-protein spectroscopy, is maximal at 357±5 nm and significantly blue-shifted compared to ferric heme nitrosyl proteins (maxima between 408 and 422 nm). This is in stark contrast to the Q-band absorption where the protein microenvironment is nearly innocent in perturbing the electronic structure of the porphyrin macrocycle. Photodissociation is primarily through loss of NO. In contrast to the Q-band region, two-photon absorption was seen in the Soret band despite NO loss only requiring ∼1 eV. A model based on intersystem crossing to a long-lived triplet state where a barrier has to be surmounted is suggested. Finally, we summarise the measured absorption maxima of heme and its complexes with amino acids and NO.
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