Reference health
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
38/38 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
8 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 38 checked references that resolve
resolves10.1016/B978-0-12-152515-6.50009-6
Evolution of a Regulatory Enzyme: Cytochrome-c Oxidase (Complex IV)
resolves10.1021/bi00198a044
Thermodynamic and Structural Stability of Cytochrome c Oxidase from Paracoccus denitrificans
resolves10.1007/BF00762850
Probing heart cytochromec oxidase structure and function by infrared spectroscopy
resolves10.1073/pnas.77.1.196
A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.
resolves10.1016/S0006-3495(91)82067-7
Comparison of energy-transducing capabilities of the two- and three-subunit cytochromes aa3 from Paracoccus denitrificans and the 13-subunit beef heart enzyme
resolves10.1002/j.1460-2075.1989.tb08529.x
Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase.
resolves10.1002/j.1460-2075.1991.tb07731.x
Subunit III of cytochrome c oxidase is not involved in proton translocation: a site‐directed mutagenesis study.
resolves10.1107/S0108768192004270
Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 Å resolution
resolves10.1111/j.1432-1033.1993.tb17865.x
Stoichiometry and redox behaviour of metals in cytochrome‐<i>c</i> oxidase
resolves10.1016/S0021-9258(19)85484-4
Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center
resolves10.1111/j.1432-1033.1992.tb17360.x
A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome <i>c</i> oxidase
resolves10.1021/bi00200a022
Metal-Metal Bonding in Biology: EXAFS Evidence for a 2.5 .ANG. Copper-Copper Bond in the CuA Center of Cytochrome Oxidase
resolves10.1002/j.1460-2075.1992.tb05398.x
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.
resolves10.1016/S0021-9258(19)85557-6
Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c.
resolves10.1007/BF00762854
Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo
resolves10.1021/bi00091a048
Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
resolves10.1021/bi00013a035
Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp135.fwdarw.Asn
resolves10.1021/bi00023a004
Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides
resolves10.1016/0005-2728(94)90093-0
Mechanism of proton translocation by the respiratory oxidases. The histidine cycle
resolves10.1007/BF00831534
The histidine cycle: A new model for proton translocation in the respiratory heme-copper oxidases
resolves10.1016/0005-2728(94)90130-9
Proton uptake by cytochrome c oxidase on reduction and on ligand binding
resolves10.1038/338776a0
Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping
resolves10.1016/S0005-2728(05)80204-X
Characterisation of ‘fast’ and ‘slow’ forms of bovine heart cytochrome-c oxidase
resolves10.1107/S0021889883010973
A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography
resolves10.1038/355472a0
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
resolves10.1107/S0108767390010224
Improved methods for building protein models in electron density maps and the location of errors in these models
resolves10.1016/0014-5793(90)80609-M
Are there isoenzymes of cytochrome <i>c</i> oxidase in <i>Paracoccus denitrificans</i>?
resolves10.1126/science.235.4787.458
Crystallographic
<i>R</i>
Factor Refinement by Molecular Dynamics
resolves10.1002/bip.360221211
Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
resolves10.1107/S0021889891004399
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
The 8 references without a DOI — listed, not checked
no DOI — not checkedTurba, A., Jetzek, M. & Ludwig, B. Eur. J. Biochem. 231, 259–265 (1995).
no DOI — not checkedSteffens, G. J. & Buse, G. Hoppe-Seyler's Z. physiol. Chem. 360, 613–619 (1979).
no DOI — not checkedRich, P. R. Aust. J. Pl. Physiol. 22, 479–486 (1994).
no DOI — not checkedOtwinowski, Z. in Proc. CCP4 Study Weekend, 29–30 Jan 1993, Data collection and Processing (eds Sawer, L., Isaacs. N. & Bailey, S.) 56–62 (SERC Daresbury Laboratory, Warrington. 1993).
no DOI — not checkedOtwinowski, Z. in Proc. CCP4 Study Weekend, 25–26 Jan 1991, Isomorphous Replacement and Anomalous Scattering (eds Wolf, W., Evans, P. R. & Leslie, A. G. W.) 80–86 (SERC Daresbury Laboratory, Warrington, 1991).
no DOI — not checkedCowtan, K. in Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34–38 (1994).
no DOI — not checkedEssen, L. O. thesis. Johann Wolfgang Goethe-Univ. (1995).
no DOI — not checkedMerrit, E. A. & Murphy, M. E. P. Acta Crystallogr. D 50, 896–873 (1994).
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