Structural highlights
3o0r is a 4 chain structure with sequence from Mus musculus and Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , , , , |
Activity: | Nitric-oxide reductase (cytochrome c), with EC number 1.7.2.5 |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NORC_PSEAE] Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). [NORB_PSEAE] Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). NorB is the catalytic subunit of the enzyme complex. Shows proton pump activity across the membrane in denitrifying bacterial cells. The mononitrogen reduction is probably coupled to electron transport phosphorylation (By similarity).
Publication Abstract from PubMed
Nitric oxide reductase (NOR) is an iron-containing enzyme that catalyzes the reduction of nitric oxide (NO) to generate a major greenhouse gas, nitrous oxide (N(2)O). Here, we report the crystal structure of NOR from Pseudomonas aeruginosa at 2.7 angstrom resolution. The structure reveals details of the catalytic binuclear center. The non-heme iron (Fe(B)) is coordinated by three His and one Glu ligands, but a His-Tyr covalent linkage common in cytochrome oxidases (COX) is absent. This structural characteristic is crucial for NOR reaction. Although the overall structure of NOR is closely related to COX, neither the D- nor K-proton pathway, which connect the COX active center to the intracellular space, was observed. Protons required for the NOR reaction are probably provided from the extracellular side.
Structural basis of biological N2O generation by bacterial nitric oxide reductase.,Hino T, Matsumoto Y, Nagano S, Sugimoto H, Fukumori Y, Murata T, Iwata S, Shiro Y Science. 2010 Dec 17;330(6011):1666-70. Epub 2010 Nov 25. PMID:21109633[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hino T, Matsumoto Y, Nagano S, Sugimoto H, Fukumori Y, Murata T, Iwata S, Shiro Y. Structural basis of biological N2O generation by bacterial nitric oxide reductase. Science. 2010 Dec 17;330(6011):1666-70. Epub 2010 Nov 25. PMID:21109633 doi:10.1126/science.1195591