Evidence that a formyl-substituted iron porphyrin is the prosthetic group of myeloperoxidase: Magnetic circular dichroism similarity of the peroxidase to Spirographis heme-reconstituted myoglobin

Masanori Sono, Alma M. Brachte, Ann M. Huff, Masao Ikeda-Saito, John H. Dawson

研究成果: Article

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To probe the identity of the active site hemetype prosthetic group of myeloperoxidase, whose structure has not been established unambiguously [proposed structures are (i) a chlorin (dihydroporphyrin) or (ii) a formyl-substituted porphyrin such as present in heme a], Spirographis heme (2-formyl-4-vinyldeuteroheme IX) has been incorporated into apo-myoglobin as a possible iron porphyrin model. Comparison of parallel derivatives of these two green proteins with magnetic circular dichroism spectroscopy reveals considerable similarities between several derivatives of these proteins, including the pyridine hemochromogen, the native ferric, ferrous-oxy, and ferrous-CO forms. In contrast, the magnetic circular dichroism spectra of available iron chlorin (octaethylchlorin) model complexes in analogous ligation and oxidation states do not show any significant spectral similarities to myeloperoxidase. This finding provides important evidence in favor of a formyl-substituted porphyrin as the structure of the prosthetic group macrocycle of myeloperoxidase.

元の言語English
ページ(範囲)11148-11152
ページ数5
ジャーナルProceedings of the National Academy of Sciences of the United States of America
88
発行部数24
DOI
出版物ステータスPublished - 1991

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