Infrared evidence for the mode of binding of oxygen to iron of myoglobin from heart muscle
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Anti-leishmanial activity and cytotoxicity of a series of tris-aryl Sb(V) mandelate cyclometallate complexes
2020, Journal of Inorganic BiochemistryCitation Excerpt :The FT-IR was able to further confirm the presence of the peroxide bond in complexes 3Sr/s. A sharp signals at 1187 cm−1 that is not found in any other complex correlates to the presence of a metal – peroxide bond [42,43]. A signal at ~3500 cm−1 representative of the α-hydroxyl can also be seen, and is absent in the remaining complexes.
Structure and function of haemoglobins
2018, Blood Cells, Molecules, and DiseasesCitation Excerpt :The precise electronic structure of the FeO2 bond has been debated since the 1936 papers on this subject were first published by Pauling and Coryell [29,30,34,35,128–134]. Infrared spectroscopy of the OO bond clearly supports formal reduction of bound oxygen to superoxide; thus the νOO frequency in Hb(O2) (1107 cm− 1) [135], Mb(O2) (1103 cm− 1) [136] and synthetic (porphinato)Fe(II)(O2) complexes (1150 cm− 1) [137] are clearly in a range expected for O2− (1150–1100 cm− 1) [29,137], and not for molecular O2 (1555 cm− 1) or peroxide (O22 −; 842 cm− 1) [29]. This is consistent with the formal superoxo model, Fe(III)+(O2−), proposed by H. G. Weiss [128,129].
Nature of the FeO<inf>2</inf> bonding in myoglobin and hemoglobin: A new molecular paradigm
2006, Progress in Biophysics and Molecular BiologyStructural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy
2005, Journal of Inorganic Biochemistry