Enzymatic formation of a phosphorylated derivative of vitamin K. | Zendy

Tetsuo Watanabe | Zendy; Arnold F. Brodie | Zendy

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Enzymatic formation of a phosphorylated derivative of vitamin K.

Author(s) -

Tetsuo Watanabe,

Arnold F. Brodie

Publication year - 1966

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.56.3.940

Subject(s) - adaptation (eye) , sustainability , climate change , computer science , chemistry , environmental ethics , ecology , biology , philosophy , neuroscience

A role for naphthoquinones in oxidative phosphorylation has been demonstrated with a cell-free system from Mycobacterium phlei.1-3 The natural naphthoquinone of this microorganism, vitamin K9H, functions between the flavoprotein and cytochrome b on the NAD+-linked and malate-vitamin K reductase pathways.3' 4 Evidence has been presented for the existence of a phosphorylative site between the natural quinone and cytochrome b.2, 5, 6 Restoration of the quinone function has been shown to occur on supplementation with vitamin K, (I) to the quinone-depleted system.1' 2, 5

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