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Enzyme diversity and mosaic gene organization in denitrification

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Abstract

Denitrification is a main branch of the global nitrogen cycle. In the past ten years unravelling the underlying biochemistry and genetics has proceeded at an increasing pace. Fungal denitrification has become a new field. The biochemical investigation of denitrification has culminated in the description of the crystal structures of the two types of nitrite reductases. The N2O reductase shares with cytochrome c oxidase the CuA center as a structurally novel metal site. The cytochrome b subunit of NO reductase has a striking conservation of heme-binding transmembrane segments versus the subunit I of cytochrome c oxidase. Another putative denitrification gene product shows structural relation to the subunit III of the oxidase. N2O reductase and NO reductase may be ancestors of energy-conserving enzymes of the heme-copper oxidase superfamily. More than 30 genes for denitrification are located in a >30-kb cluster in Pseudomonas stutzeri, and comparable gene clusters have been identifi ed in Pseudomonas aeruginosa and Paracoccus denitrificans. Genes necessary for nitrite reduction and NO reduction have a mosaic arrangement with very few conserved locations within these clusters and relative to each other.

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  1. Lehrstuhl für Mikrobiologie, Universität Fridericiana, D-76128, Karlsruhe, Germany

    Walter G. Zumft & Heinz Körner

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  1. Walter G. Zumft
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Zumft, W.G., Körner, H. Enzyme diversity and mosaic gene organization in denitrification. Antonie Van Leeuwenhoek 71, 43–58 (1997). https://doi.org/10.1023/A:1000112008026

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