Photochemically Modified Myeloperoxidase, with Optical Spectral Properties Analogous to Those of Lactoperoxidase, Retains Its Original Catalytic Activity

Hiroshi Hori, Masao Ikeda-Saito

研究成果: Article査読

12 被引用数 (Scopus)

抄録

During the course of a reducing reaction using ketyl radicals generated from ketone photoreduction with ultraviolet light, a photoinduced chemical modification of the chromophore group in myeloperoxidase has been found. Light absorption and resonance Raman spectra for this modified enzyme indicated an iron porphyrin chromophore group. The alkaline pyridine hemochrome of the modified enzyme exhibited an optical spectrum closely related to that of iron protoporphyrin IX. The chromophore group of the modified myeloperoxidase was cleaved from the protein by methoxide. Proton magnetic resonance of the diamagnetic bis(cyanide) compound of the extracted heme group showed the presence of two vinyl and three methyl side chains associated with a porphyrin macrocycle. These data provide further insight into the structure of the active site in myeloperoxidase. The EPR spectral properties and enzymatic activities of the native myeloperoxidase are essentially conserved in the modified enzyme. Our present results indicate that the heme peripheral substituent is modified while the stereochemical structure surrounding the chromophore group is not altered by the photochemical modification.

本文言語English
ページ(範囲)7106-7112
ページ数7
ジャーナルBiochemistry
29
30
DOI
出版ステータスPublished - 1990 7 1

ASJC Scopus subject areas

  • 生化学

フィンガープリント

「Photochemically Modified Myeloperoxidase, with Optical Spectral Properties Analogous to Those of Lactoperoxidase, Retains Its Original Catalytic Activity」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル