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Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism.

Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Research Abstract Details 

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  • Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Abstract Text:

    t yoshidaT Yoshida,m noguchiM Noguchi,g kikuchiG Kikuchi,s sanoS Sano,

    Mesoheme bound to heme oxygenase protein was easily degraded to mesobiliverdin by incubation with NADPH-cytochrome c reductase and NADPH. The features of mesoheme degradation were very similar to those of protoheme degradation catalyzed by the heme oxygenase system; an intermediate compound having its absorption maximum at 660 nm appeared in the couse of mesoheme degradation and this compound is presumably equivalent to the 688 nm compound which appears in the course of protoheme degradation. Hydroxymesoheme was chemically prepared and a complex of hydroxymesoheme and heme oxygenase was prepared. The complex was fairly stable in air, but when the complex was incubated with the NADPH-cytochrome c reductase system, the hydroxymesoheme bound to heme oxygenase was readily converted to mesobiliverdin through the 660 nm compound as an intermediate. It is evident that hydroxyheme is a real intermediate of heme degradation in the heme oxygenase reaction and that the 688 nm compound (or the 660 nm compound in the mesoheme system) is located between hydroxyheme and the biliverdin-iron chelate. The ferrous state of heme-iron may also be necessary for the onset of further oxidation of hydroxyheme.

    Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Publishing Authors By Initials

    t yoshidaT Yoshida,m noguchiM Noguchi,g kikuchiG Kikuchi,s sanoS Sano,

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

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    Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 90

    Page Numbers: 125-31

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jul

    YEAR: 1981

    Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Keywords Mesh Terms:

    KEYWORDS: Swine

    MESH TERMS: enzymology

    Chemical & Substance for Abstract: Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. Information

    Substance Name: Heme Oxygenase (Decyclizing)

    Registry Number: EC 1.14.99.3

    Grant and Affiliation Information for Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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