Overview for MACiE Entry M0004
EC Number: 22.214.171.124 (A member of the Oxidoreductases, Acting on other nitrogenous compounds as donors, With a cytochrome as acceptor)
Enzyme Name: nitrite reductase (NO-forming)
Biological Species: Achromobacter cycloclastes (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- P25006 - Copper-containing nitrite reductase
Representative PDB Code: 1nia - THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTERCYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND ANDWITH TYPE II CU DEPLETED (Resolution = 2.50 Å).
Catalytic CATH Codes:
"Other" CATH Codes:
Display structure information
It is unknown whether this reaction is reversible or not.
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Stepwise Description of the Reaction
|Step 1||Pseudoazurin donates an electron, through Cu501, Cys136 and His135 to Cu502.|
|Step 2||Cu502 donates the electron to the bound nitrous acid, which collapses to form water, deprotonating His255B, and a Cu-bound NO radical.|
|Step 3||Water displaces the NO radical, and is deprotonated by His255B, to regenerate the enzyme's resting state.|
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Catalytic Residues Involved
||Location of Function
Main Chain Carbonyl
Main Chain Amide
Metal Cofactors for M0004
- M. J. Boulanger et al. (2000), J. Biol. Chem., 275, 23957-23964. Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase.
- S. V. Antonyuk et al. (2005), Proc. Natl Acad. Sci. USA, 102, 12041-12046. Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism.
- S. Suzuki et al. (2000), Acc. Chem. Res., 33, 728-735. Metal coordination and mechanism of multicopper nitrite reductase.
- E. I. Tocheva et al. (2004), Science, 304, 867-870. Side-on copper-nitrosyl coordination by nitrite reductase.
- T. Inoue et al. (1999), J. Biol. Chem., 274, 17845-17852. Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine.
Homologue information for M0004 (1nia)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Entries with at least one Catalytic CATH code in common (different mechanisms):
|M0278 ||plastoquinol-plastocyanin reductase |
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