Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus (Q27622302)

2

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G P Bourenkov

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H D Bartunik

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R Huber

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M E Than

The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution

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language of work or name

English

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publication date

17 April 2000

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published in

The EMBO Journal

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volume

19

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issue

8

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page(s)

1766-76

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cites work

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Electrochemical, FTIR, and UV/VIS Spectroscopic Properties of theba3Oxidase fromThermus thermophilus†

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12 December 2020

Proton translocation by cytochrome c oxidase

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The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance raman spectroscopy

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Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase

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Heme/Copper Terminal Oxidases

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 A resolution

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12 December 2020

Proton uptake by cytochrome c oxidase on reduction and on ligand binding

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Channelling of dioxygen into the respiratory enzyme

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Cytochrome-c552 from Thermus thermophilus: a functional and crystallographic investigation

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Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-cOxidase inParacoccus denitrificans

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Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans

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Cyanide binding and active site structure in heme-copper oxidases: normal coordinate analysis of iron-cyanide vibrations of a3(2+)CN- complexes of cytochromes ba3 and aa3

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12 December 2020

Identifiers

DOI

10.1093/EMBOJ/19.8.1766

1 reference

1 reference

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PubMed publication ID

10775261

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