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Global Journal of Inorganic Chemistry 2012, 3: 1
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Review Article
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NMR studies on the electronic structure of green hemes and
green heme proteins
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Mikio Nakamuraa,b
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a Department of Chemistry, Faculty of Medicine, Toho University, Ota-ku, Tokyo 143-8540, Japan
b Division of Chemistry, Graduate School of Science, Toho University, Funabashi 274-8510, Japan
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Abstract |
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Green hemes are the iron complexes of hydroporphyrins such as chlorin, bacteriochlorin, and isobacteriochloin. Green heme proteins are enzymes that contain green heme such as heme d, heme d1, and siroheme as prosthetic groups. These proteins are playing a number of important roles such as the reduction of oxygen, nitrite and sulfite as well as the dismutation of hydrogen peroxide. In contrast to the heme proteins which have been extensively studied by various spectroscopic, magnetic, and crystallographic methods, the studies on the green heme proteins are far from enough. This review focuses the NMR studies on the green hemes and green heme proteins, and describes the relationship between the NMR chemical shifts and the electronic structures including the oxidation states, spin states, and electron configurations.
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Keywords |
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NMR spectra; Hydroporhyrins; Chlorins; Isobacteriochlorins; Green hemes; Electronic structure; Spin state, Oxidation state
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