Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions (Q62552060)

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scientific article published on 01 December 1998

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English	Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions	scientific article published on 01 December 1998

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scholarly article

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7 December 2019

Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions (English)

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7 December 2019

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H Michel

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C Ostermeier

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B Ludwig

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W Mäntele

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1 December 1998

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Biochimica et Biophysica Acta

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1409

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107-112

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7 December 2019

Heme/Copper Terminal Oxidases

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Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment

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Subunit III of cytochrome c oxidase is not involved in proton translocation: a site-directed mutagenesis study

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Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans.

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The effect of N,N'-dicyclohexylcarbodiimide on enzymes of bioenergetic relevance.

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Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane-potential measurements with the two-subunit and three-subunit enzyme

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Channelling of dioxygen into the respiratory enzyme

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Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans

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Subunit III of Cytochrome c Oxidase Influences the Conformation of Subunits I and II: An Infrared Study

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Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy

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7 January 2021

Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy†

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Redox Dependent Changes at the Heme Propionates in CytochromecOxidase fromParacoccusdenitrificans: Direct Evidence from FTIR Difference Spectroscopy in Combination with Heme Propionate13C Labeling†

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Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase

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Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c.

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Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans.

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7 January 2021

Isolation, analysis, and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans.

1 reference

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7 January 2021

Involvement of cytochrome c oxidase subunit III in energy coupling

1 reference

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7 January 2021

Comparison of energy-transducing capabilities of the two- and three-subunit cytochromes aa3 from Paracoccus denitrificans and the 13-subunit beef heart enzyme

1 reference

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7 January 2021

Identifiers

10.1016/S0005-2728(98)00151-0

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Europe PubMed Central

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7 December 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9838069%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

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