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

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About: Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1998

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1998 (uk) article scientifique publié en 1998 (fr) artículu científicu espublizáu en mayu de 1998 (ast) scientific article published on 01 May 1998 (en) im Mai 1998 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q62552069-F23D4D0D-5F34-4930-93B3-93DB0CBB4238
publication date	1998-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q62552069-4F8FEA3C-5C93-4CC8-BFE6-86DE4131C41F
language of work or name	English
cites work	wds:Q62552069-060AA631-75B4-400D-94C8-7EC3F16A9C2E wds:Q62552069-2F2A3F3B-3E66-450F-B435-4FCF47D299A1 wds:Q62552069-31B4DFA9-C583-4B1B-AD61-8456E6E2B48C wds:Q62552069-5621E290-1870-4A2D-B9FF-D1FFFF2FEB78 wds:Q62552069-7FB50580-F6B3-400B-B91E-196D05D512F2 wds:Q62552069-87F5F501-E5AC-4328-ABD8-870AB215E3B2 wds:Q62552069-9F3E3288-9E8F-4B33-80CC-CF6CA20D30A0 wds:Q62552069-ABADCAA8-12B0-4ED7-87CC-DCEB9C9099BB wds:Q62552069-B1A8A1B8-7B6B-48A1-AF33-035BEAA713FB
cites work	A re-evaluation of the spectral, potentiometric and energy-linked properties of cytochromecoxidase in mitochondria FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model Heme/Copper Terminal Oxidases Photoperturbation of the heme a3-CuB binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy The histidine cycle: a new model for proton translocation in the respiratory heme-copper oxidases Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases. Electron transfer between cytochrome c and the isolated CuA domain: identification of substrate-binding residues in cytochrome c oxidase. Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy Site-directed mutagenesis of cytochrome c oxidase reveals two acidic residues involved in the binding of cytochrome c
author name string	wds:Q62552069-3099D66C-C71D-40B0-8926-D7B465957FAA wds:Q62552069-36F6FEF6-9C69-468C-B295-D44E46D2E599 wds:Q62552069-3BA028E6-216F-4FB0-BB77-52855220278F wds:Q62552069-4094CCBC-00A8-4339-BE50-3C21C2324127 wds:Q62552069-83E79DDC-0B22-4198-A8FB-2D789DE1ABBD wds:Q62552069-C1E8AF8F-411C-4C63-83FB-D58E91D4D530 wds:Q62552069-E1A41D8C-5827-406F-A983-F88FA185FC03
author name string	Mäntele W Behr J Ludwig B Ostermeier C Odenwald A Pfitzner U Richter OM
rdfs:label	Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (en) Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (nl)
skos:prefLabel	Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (en) Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (nl)
name	Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (en) Involvement of Glutamic Acid 278 in the Redox Reaction of the CytochromecOxidase fromParacoccus denitrificansInvestigated by FTIR Spectroscopy† (nl)
author	wds:Q62552069-8636AF18-4DBE-4853-9A5C-7657B6BC23D1 wds:Q62552069-92682069-E50A-4A9A-BAB3-6671D99105F3
author	Hartmut Michel Petra Hellwig
title	wds:Q62552069-95C61F7C-32DE-4A26-B800-53886B7CDF2A
title	Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy (en)
page(s)	wds:Q62552069-7AB56832-E40B-49FD-90D4-2B7A1569876F
page(s)	7390-7399
instance of	wds:Q62552069-F79AC99E-65F8-4D41-94A3-8A7FFA5B404D
instance of	scholarly article
main subject	wds:Q62552069-9E949315-2974-443B-896E-83994BCD37BF wds:Q62552069-FE34C87C-B70B-49D8-8F54-7AE2E0A458A9
main subject	Paracoccus denitrificans spectroscopy
PubMed ID	wds:Q62552069-F13746DE-B60A-4D61-948F-CF88723D027E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9585553
PubMed ID	9585553
published in	wds:Q62552069-01EF1230-4204-46BD-B127-C0D1F89D8C7A
published in	Biochemistry
issue	wds:Q62552069-891E7213-2ED0-44D8-81A7-8E278AD3CA6D
volume	wds:Q62552069-C235E8E6-5B9F-4E63-A87F-CCC78A9FAEBF
issue	20
volume	37
DOI	wds:Q62552069-CBF17BF9-176D-424B-909F-407A0B427048
DOI	http://dx.doi.org/10.1021/BI9725576
DOI	10.1021/BI9725576
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q62552069
is cites work of	Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase Proton translocation by bacteriorhodopsin and heme-copper oxidases Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I). Steady-state and time resolved fluorescence analysis on tyrosine-histidine model compounds Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase Bioenergetics of the Archaea Redox-driven proton pumping by heme-copper oxidases The role of electrostatics in proton-conducting membrane protein complexes Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers Structure and dynamics of membrane proteins as studied by infrared spectroscopy Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins Transient binding of CO to Cu(B) in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation The mechanism of proton pumping by cytochrome c oxidasex127e [comments] Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site Fungal respiration: a fusion of standard and alternative components Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase Intramolecular electron transfer in sulfite-oxidizing enzymes: probing the role of aromatic amino acids A novel scenario for the evolution of haem-copper oxygen reductases. Cytochrome c oxidase: exciting progress and remaining mysteries Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase 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 Similarities and dissimilarities in the structure-function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy Where is 'outside' in cytochrome c oxidase and how and when do protons get there? Structures of reaction intermediates of bovine cytochrome c oxidase probed by time-resolved vibrational spectroscopy

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