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Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum.

Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Research Abstract Details 

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  • Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Abstract Text:

    k tanakaK Tanaka,t kakunoT Kakuno,j yamashitaJ Yamashita,t horioT Horio,

    1. The chlorophyllase [EC 3.1.1.14] purified from greened rye seedlings hydrolyzed the bacteriochlorophyll isolated from Rhodospirillum rubrum, but not the pigment bound to the membrane of chromatophores or spheroplasts from the bacterium. 2. Acetone, if added at such concentrations that the bound bacteriochlorophyll would not be solubilized, enabled the enzyme to hydrolyze the bound pigment. The acetone concentrations required for half the maximum hydrolysis rates were 16% with chromatophores and 7% with spheroplasts. 3. The enzymic hydrolysis of the bound bacteriochlorophyll in the presence of acetone removed bacteriochlorophyllide from the membrane, leaving its esterifying alcohol, possibly all-trans-geranylgeraniol, in situ. 4. Washing of chromatophores with 30% acetone removed about 10% of the bound bacteriochlorophyll. The bound pigment remaining after washing was not hydrolyzed by the enzyme unless acetone was added. 5. It seems possible that light-harvesting bacteriochlorophyll was mostly, if not all, bound to the inner surface of chromatophores (the outer surface of spheroplasts), having its esterifying alcohol residue buried in the membrane and its porphyrin residue emerging from the membrane into the inside solution; thus, chlorophyllase could not make contact with the ester linkage between the esterifying alcohol and porphyrin moieties of the pigment unless the esterifying alcohol residue was partly exposed.

    Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Publishing Authors By Initials

    k tanakaK Tanaka,t kakunoT Kakuno,j yamashitaJ Yamashita,t horioT Horio,

    For similar cells: spheroplasts research abstracts see: cells: spheroplasts research

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    Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 93

    Page Numbers: 159-67

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jan

    YEAR: 1983

    Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Keywords Mesh Terms:

    KEYWORDS: Spheroplasts

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum. Information

    Substance Name: chlorophyllase

    Registry Number: EC 3.1.1.14

    Grant and Affiliation Information for Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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    Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum Related Publications

     

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