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In enzymology, a camphor 1,2-monooxygenase (EC 1.14.15.2) is an enzyme that catalyzes the chemical reaction

(+)-bornane-2,5-dione + reduced rubredoxin + O₂ ${\displaystyle \rightleftharpoons }$ 5-oxo-1,2-campholide + oxidized rubredoxin + H₂O

The 3 substrates of this enzyme are (+)-bornane-2,5-dione, reduced rubredoxin, and O₂, whereas its 3 products are 5-oxo-1,2-campholide, oxidized rubredoxin, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,2-lactonizing). Other names in common use include 2,5-diketocamphane lactonizing enzyme, camphor ketolactonase I, oxygenase, camphor 1,2-mono, and ketolactonase I. It employs one cofactor, iron.

References

• Conrad HE, Dubus R, Namtvedt MJ, Gunslaus IC (1965). "Mixed Function Oxidation. II. Separation and Properties of the Enzymes Catalyzing Camphor Lactonization". Journal of Biological Chemistry. 240: 495–503. PMID 14253460.
• Trudgill PW, DuBus R, Gunsalus IC (1966). "Mixed function oxidation. VI. Purification of a tightly coupled electron transport complex in camphor lactonization". Journal of Biological Chemistry. 241 (18): 4288–90. PMID 4288652.
• Yu CA, Gunsalus IC (1969). "Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components". Journal of Biological Chemistry. 244 (22): 6149–52. PMID 4310834.

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