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Structure and assembly of protocatechuate 3,4-dioxygenase

Nature volume 336, pages 403–405 (1988)Cite this article

Abstract

Dioxygenases catalyse the cleavage of molecular oxygen with subsequent incorporation of both oxygen atoms into organic substrates. Some of the best-studied dioxygenases have been isolated from bacteria where they catalyse the critical ring-opening step in the biodegradation of aromatic compounds. These bacterial enzymes generally contain nonheme ferric iron as the sole cofactor. Protocatechuate 3,4-dioxygenase (3,4-PCD) was one of the first such enzymes recognized1 and catalyses the intradiol cleavage of protocatechuic acid by oxygen to produce β- car boxy- cis,cis-muconic acid. Previous studies have shown that the 3,4-PCD found in Pseudomonas aeruginosa is an oligomer with a relative molecular mass (Mr) of 587,000 (587K) containing 12 copies each of α (22.3K) and β (26.6K) subunits2–6. The X-ray structure determination of 3,4-PCD reveals the catalytic iron environment required for oxygenolytic cleavage of aromatic rings and also provides a novel holoenzyme assembly with cubic 23(T) symmetry and first examples of mixed β-barrel domains.

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Authors and Affiliations

  1. E. I. du Pont de Nemours and Co., Central Research and Development Department, Experimental Station, PO Box 80228, Wilmington, Delaware, 19880-0228, USA

    D. H. Ohlendorf & P. C. Weber

  2. Department of Biochemistry, University of Minnesota, 4-225 Millard Hall, Minneapolis, Minnesota, 55455, USA

    J. D. Lipscomb

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  1. D. H. Ohlendorf
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  2. J. D. Lipscomb
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  3. P. C. Weber
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Ohlendorf, D., Lipscomb, J. & Weber, P. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature 336, 403–405 (1988). https://doi.org/10.1038/336403a0

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