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Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction.

Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Research Abstract Details 

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  • Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Abstract Text:

    t yoshidaT Yoshida,m noguchiM Noguchi,

    The degradation of protoheme in the heme oxygenase reaction involves three oxidation steps: from protoheme to hydroxyheme, from hydroxyheme to a 688-nm substance, a protein-bound intermediate, and from the 688-nm substance to a biliverdin-iron complex. The 688-nm substance has a ferrous iron and it readily binds carbon monoxide to form a CO-complex, called the 638-nm substance (Yoshida, T., Noguchi, M., & Kikuchi, G. (1980) J. Biochem. 88, 557-563). The ferric 688-nm substance was prepared from the 638-nm substance by the addition of potassium ferricyanide together with aspiration to eliminate CO. The ferric 688-nm substance did not show any distinct absorption maximum in the red region of the absorption spectrum. The ferric 688-nm substance was readily reduced on the addition of the NADPH-cytochrome P-450 reductase system, but the ferric 688-nm substance could also be reduced spontaneously though at a very low rate. The ferrous 688-nm substance free from excess reducing agents was prepared by passing the 638-nm substance through a column of Sephadex G-25. The ferrous 688-nm substance was degraded to a biliverdin-iron complex much more rapidly in the presence of the NADPH-cytochrome P-450 reductase system than in its absence, indicating that a reducing equivalent is essential for the initiation of heme degradation even when starting from the ferrous 688-nm substance. Cyanide was found to bind to the ferrous 688-nm substance to form a stable compound; the cyanide compound formed could revert to neither the ferrous 688-nm substance nor the 638-nm substance.(ABSTRACT TRUNCATED AT 250 WORDS)

    Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Publishing Authors By Initials

    t yoshidaT Yoshida,m noguchiM Noguchi,

    For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

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    Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 96

    Page Numbers: 563-70

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Aug

    YEAR: 1984

    Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Keywords Mesh Terms:

    KEYWORDS: Swine

    MESH TERMS: enzymology

    Chemical & Substance for Abstract: Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. Information

    Substance Name: NADPH-Ferrihemoprotein Reductase

    Registry Number: EC 1.6.2.4

    Grant and Affiliation Information for Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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