Publication
Probing the Electronic Structure of the Hemoglobin Active Center in Physiological Solutions
Abstract
Soft-x-ray absorption spectroscopy at the L2,3 edge of the iron center in bovine Hb and hemin under physiol. conditions is reported for the first time. Spectra of the same compds. in solid form are presented for comparison. Striking differences in the electronic structure of the metalloporphyrin are obsd. between the liq. and solid compds. We unambiguously show that Hb and hemin are in a high-spin ferric state in soln., and that the 2p spin-orbit coupling decreases for hemin compared to the Hb, while this is not the case in solids. The spectra were simulated using ligand field multiplet theory, in good agreement with the expt., allowing quantification of the amt. of charge transfer between the porphyrin and Fe3+ ion in Hb and in hemin.
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Ontological neighbourhood
Related concepts (33)
Iron
Iron is a chemical element with the symbol Fe () and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, just ahead of oxygen (32.1% and 30.1%, respectively), forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust, being mainly deposited by meteorites in its metallic state, with its ores also being found there.
X-ray spectroscopy
X-ray spectroscopy is a general term for several spectroscopic techniques for characterization of materials by using x-ray radiation. When an electron from the inner shell of an atom is excited by the energy of a photon, it moves to a higher energy level. When it returns to the low energy level, the energy which it previously gained by the excitation is emitted as a photon which has a wavelength that is characteristic for the element (there could be several characteristic wavelengths per element).
Iron-sulfur protein
Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts.
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