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The study focuses on the purification and characterization of the terminal oxygenase component B of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816, which oxidizes naphthalene to a specific dihydroxy derivative. Component B, an iron-sulfur protein, was purified and shown to require NADH, oxygen, and other components for activity, with a molecular weight of approximately 158,000 and a quaternary structure of a2cB2. The findings suggest that this component plays a crucial role in the terminal st

Author
Sancho Rajan
Language
EN

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