pubmed.ncbi.nlm.nih.gov

Pseudomonas stutzeri N2O reductase contains CuA-type sites - PubMed

Comparative Study

Pseudomonas stutzeri N2O reductase contains CuA-type sites

R A Scott et al. Proc Natl Acad Sci U S A. 1989 Jun.

Erratum in

Proc Natl Acad Sci U S A 1989 Dec;86(23):9278

Abstract

N2O reductase (N2O----N2) is the terminal enzyme in the energy-conserving denitrification pathway of soil and marine denitrifying bacteria. The protein is composed of two identical subunits and contains eight copper ions per enzyme molecule. The magnetic circular dichroism spectrum of resting (oxidized) N2O reductase is strikingly similar to the magnetic circular dichroism spectrum of the CuA site in mammalian cytochrome c oxidase [Greenwood, C., Hull, B. C., Barber, D., Eglinton, D. G. & Thomson, A. J. (1983) Biochem. J. 215, 303-316] and is unlike the magnetic circular dichroism spectra of all other biological copper chromophores obtained to date. Sulfur (or chlorine) scatterers are required to fit the copper extended x-ray absorption fine structure data of both the oxidized and reduced forms of N2O reductase. Satisfactory fits require a Cu-N or Cu-O [denoted Cu-(N, O)] interaction at 2.0 A, a Cu-(S, Cl) interaction at 2.3 A and an additional Cu(S, Cl) interaction at approximately 2.6 A (oxidized) or approximately 2.7 A (reduced). Approximately eight sulfur ions (per eight copper ions) at approximately 2.3 A are required to fit the extended x-ray absorption fine structure data for both the oxidized and reduced N2O reductase. The 2.3-A Cu-(S, Cl) distance is nearly identical to that previously determined for the CuA site in cytochrome c oxidase. A 2.6-2.7 A Cu-(S, Cl) interaction is also present in resting and fully reduced cytochrome c oxidase. Comparison of the N2O reductase sequence, determined by translating the structural NosZ gene, with cytochrome c oxidase subunit II sequences from several sources indicates that a Gly-Xaa-Xaa-Xaa-Xaa-Xaa-Cys-Ser-Xaa-Xaa-Cys-Xaa-Xaa-Xaa-His stretch is highly conserved. This sequence contains three of the probable ligands (two cysteines and one histidine) in a CuA-type site. Collectively these data establish that Pseudomonas stutzeri N2O reductase contains CuA-type sites.

PubMed Disclaimer

Cited by

The effect of pH on Marinobacter hydrocarbonoclasticus denitrification pathway and nitrous oxide reductase.
Carreira C, Nunes RF, Mestre O, Moura I, Pauleta SR. Carreira C, et al. J Biol Inorg Chem. 2020 Oct;25(7):927-940. doi: 10.1007/s00775-020-01812-0. Epub 2020 Aug 26. J Biol Inorg Chem. 2020. PMID: 32851479
Cytochrome oxidase as a proton pump.
Wilson MT, Bickar D. Wilson MT, et al. J Bioenerg Biomembr. 1991 Oct;23(5):755-71. doi: 10.1007/BF00786000. J Bioenerg Biomembr. 1991. PMID: 1660873 Review.
Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.
van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmström BG, et al. van der Oost J, et al. EMBO J. 1992 Sep;11(9):3209-17. doi: 10.1002/j.1460-2075.1992.tb05398.x. EMBO J. 1992. PMID: 1324168 Free PMC article.
Cu(A) centers and their biosynthetic models in azurin.
Savelieff MG, Lu Y. Savelieff MG, et al. J Biol Inorg Chem. 2010 May;15(4):461-83. doi: 10.1007/s00775-010-0625-2. Epub 2010 Feb 19. J Biol Inorg Chem. 2010. PMID: 20169379 Review.
The superfamily of heme-copper respiratory oxidases.
García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB. García-Horsman JA, et al. J Bacteriol. 1994 Sep;176(18):5587-600. doi: 10.1128/jb.176.18.5587-5600.1994. J Bacteriol. 1994. PMID: 8083153 Free PMC article. Review. No abstract available.

References

1. Eur J Biochem. 1985 Dec 16;153(3):459-67 - PubMed
1. J Bacteriol. 1985 Sep;163(3):918-24 - PubMed
1. J Inorg Biochem. 1986 Oct-Nov;28(2-3):195-205 - PubMed
1. J Biol Chem. 1987 May 15;262(14):6515-25 - PubMed
1. Biochemistry. 1987 Apr 21;26(8):2091-5 - PubMed

Pseudomonas stutzeri N2O reductase contains CuA-type sites - PubMed