The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from Achromobacter cycloclastes
Abstract
The three-dimensional crystal structure of the copper-containing nitrite reductase (NIR) from Achromobacter cycloclastes has been determined to 2.3 angstrom (Å) resolution by isomorphous replacement. The monomer has two Greek key β-barrel domains similar to that of plastocyanin and contains two copper sites. The enzyme is a trimer both in the crystal and in solution. The two copper atoms in the monomer comprise one type I copper site (Cu-I; two His, one Cys, and one Met ligands) and one putative type II copper site (Cu-II; three His and one solvent ligands). Although ligated by adjacent amino acids Cu-I and Cu-II are ∼12.5 Å apart. Cu-II is bound with nearly perfect tetrahedral geometry by residues not within a single monomer, but from each of two monomers of the trimer. The Cu-II site is at the bottom of a 12 Å deep solvent channel and is the site to which the substrate (NO 2 - ) binds, as evidenced by difference density maps of substrate-soaked and native crystals.
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Metadata
- Authors
- Godden, J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., Payne, W. J., & LeGall, J.
- Venue
- Science
- Published
- 1991-07-26
- Volume
- 253
- Issue
- 5018
- Pages
- 438-442
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1980711521
- Cited by
- 360
- References
- 20
- FWCI
- 21.04
- Type
- journal article
- Language
- en
- Open access
- closed
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- Godden, J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., Payne, W. J., & LeGall, J. (1991). The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from Achromobacter cycloclastes. Science. https://doi.org/10.1126/science.1862344
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