The catalytic mechanism of Pseudomonas aeruginosa cd1 nitrite reductase

Biochem Soc Trans. 2011 Jan;39(1):195-200. doi: 10.1042/BST0390195.


The cd1 NiRs (nitrite reductases) are enzymes catalysing the reduction of nitrite to NO (nitric oxide) in the bacterial energy conversion denitrification process. These enzymes contain two distinct redox centres: one covalently bound c-haem, which is reduced by external electron donors, and another peculiar porphyrin, the d1-haem (3,8-dioxo-17-acrylate-porphyrindione), where nitrite is reduced to NO. In the present paper, we summarize the most recent results on the mechanism of nitrite reduction by the cd1 NiR from Pseudomonas aeruginosa. We discuss the essential catalytic features of this enzyme, with special attention to the allosteric regulation of the enzyme's activity and to the mechanism employed to avoid product inhibition, i.e. trapping of the active-site reduced haem by the product NO. These results shed light on the reactivity of cd1 NiRs and assign a central role to the unique d1-haem, present only in this class of enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Catalytic Domain
  • Denitrification
  • Electrons
  • Heme / analogs & derivatives
  • Heme / chemistry
  • Heme / metabolism
  • Molecular Structure
  • Nitrite Reductases / metabolism*
  • Nitrites / metabolism*
  • Protein Conformation
  • Pseudomonas aeruginosa / enzymology*


  • Bacterial Proteins
  • Nitrites
  • Heme
  • heme d1
  • Nitrite Reductases