Methods in Enzymology Vol.188 Hydrocarbons and Methylotrophy

Discussion in 'Methods in Enzymology Book Series' started by admin, Jul 24, 2016.

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    admin Thư Viện Sách Việt Staff Member Quản Trị Viên

    The enzyme system from Pseudomonas oleovorans that catalyzes the hydroxylation of terminal methyl groups of alkanes and fatty acids was first shown by Coon and co-workers to consist of three protein components: rubredoxin; NADH: rubredoxin reductase; and a monooxygenase protein which they named "to-hydroxylase." ~-7 Rubredoxin, a red ironsulfur protein of molecular weight 19,000, which contains no labile sulfide and which exhibits an electron paramagnetic resonance (EPR) spectrum characteristic of high-spin ferric in a rhombic field, has been shown to function as an electron carrier in the system. The reductase is a 55,000 molecular weight flavoprotein, whereas the to-hydroxylase has proved to be relatively insoluble and unstable, easily aggregated to a molecular weight of 2 × 10~, and difficult to purify. It has been characterized as a nonheme iron protein, with one iron atom and one cysteine per 40,800 molecular weight polypeptide chain, containing a high concentration of phospholipid plus carbohydrate.
    • Series: Methods in Enzymology (Book 188)
    • Hardcover: 504 pages
    • Publisher: Academic Press;
    • Language: English
    • ISBN-10: 0121820890
    • ISBN-13: 978-0121820893
    • Product Dimensions: 6 x 1.2 x 9 inches
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    Last edited: Dec 4, 2021

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