1GJQ

Pseudomonas aeruginosa cd1 nitrite reductase reduced cyanide complex

Summary for 1GJQ

• Entry DOI: 10.2210/pdb1gjq/pdb
• Related: 1BL9 1N15 1N50 1N90 1NIR 1NNO
• Descriptor: NITRITE REDUCTASE, HEME C, HEME D, ... (5 entities in total)
• Functional Keywords: reductase, oxidoreductase, electron transport, heme
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 2
• Total formula weight: 123232.11

Authors

Nurizzo, D.,Brown, K.,Tegoni, M.,Cambillau, C. (deposition date: 2001-08-01, release date: 2002-08-01, Last modification date: 2023-12-13)

Primary citation

Sun, W.,Arese, M.,Brunori, M.,Nurizzo, D.,Brown, K.,Cambillau, C.,Tegoni, M.,Cutruzzola, F.
Cyanide Binding to Cd(1) Nitrite Reductase from Pseudomonas Aeruginosa: Role of the Active-Site His369 in Ligand Stabilization.
Biochem.Biophys.Res.Commun., 291:1-, 2002

PubMed Abstract: Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite reductase (Pa cd(1) NiR) has been investigated for the wild-type enzyme and a site-directed mutant in which the active-site His369 was replaced by Ala. This mutation reduces the affinity toward cyanide (by approximately 13-fold) and especially decreases the rate of binding of cyanide to the reduced d(1) heme (by approximately 100-fold). The crystal structure of wild-type reduced Pa cd(1) NiR saturated with cyanide was determined to a resolution of 2.7 A. Cyanide binds to the iron of the d(1) heme, with an Fe-C-N angle of 168 degrees for both subunits of the dimer and only His369 is within hydrogen bonding distance of the nitrogen atom of the ligand. These results suggest that in Pa cd(1) NiR the invariant distal residue His369 plays a dominant role in controlling the binding of anionic ligands and allow the discussion of the mechanism of cyanide binding to the wild-type enzyme.

PubMed: 11829453
DOI: 10.1006/BBRC.2002.6391

Experimental method

X-RAY DIFFRACTION (2.7 Å)