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 Link Download http://nitroflare.com/view/C14E22AD0FB9EA6https://drive.google.com/drive/folders/1yLBzZ1rSQoNjmWeJTZ3WGQHg04L1
