About: Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase

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About: Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1995

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1995 (uk) article scientifique publié en 1995 (fr) im Oktober 1995 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1995 (ast) scientific article published on 01 October 1995 (en)
publication date	wds:Q71816198-2BEDE406-A94C-49E7-9ACB-C1CECBC51A70
publication date	1995-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71816198-29397522-B9F5-48C7-A462-37F13B088A57
language of work or name	English
cites work	wds:Q71816198-6DB17C96-72D6-4CCB-9972-B2123862AAA9 wds:Q71816198-B438CAB4-7E17-4EF0-9C6D-C58F30B4FDD9 wds:Q71816198-C50FF683-B35E-43A5-9F8B-D5053708B5C7 wds:Q71816198-CDD24698-C563-4EEF-AB07-6CF85D6B0C3E wds:Q71816198-DBF1A9E6-30F6-4FE4-859F-612764C1A798 wds:Q71816198-DD52BB10-FCAC-4715-8786-7B58B6C06A57 wds:Q71816198-DD53FF88-77FB-4173-9F65-E6F0828EB8B1 wds:Q71816198-E4FE09FF-2515-4EEF-899B-B398ED1A959F wds:Q71816198-E5D4E275-53FF-43F1-96EE-7F8D918F882A
cites work	Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli Properties of the two terminal oxidases of Escherichia coli The happy family of cytochrome oxidases Molecular structure of a heme-copper redox center of the Escherichia coli ubiquinol oxidase: evidence and model The superfamily of heme-copper respiratory oxidases Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier transform infrared spectroscopic studies. Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo Assignment of ESR signals of Escherichia coli terminal oxidase complexes.
author name string	wds:Q71816198-6113A1A3-9FBD-457B-8A12-AF0783A793E1 wds:Q71816198-76F17C8A-0856-4F80-BD6A-E823D5DC68E1 wds:Q71816198-7789F33E-448C-477D-BDCA-2A7A6F572C7F wds:Q71816198-CFF0DFA3-0612-48DA-AB2D-9B1BA2691C1C wds:Q71816198-E3C90581-E4BD-440B-8444-4DFCD78DADBD wds:Q71816198-EAF58403-9F63-4031-85C7-017A10FB4157
author name string	Y Anraku S Itoh H Miyoshi T Mogi K Matsuura M Sato-Watanabe
rdfs:label	Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase (en) Stabilization of a semiquinone radical at the high-affinity quinone-binding site (nl)
skos:prefLabel	Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase (en) Stabilization of a semiquinone radical at the high-affinity quinone-binding site (nl)
name	Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase (en) Stabilization of a semiquinone radical at the high-affinity quinone-binding site (nl)
title	wds:Q71816198-DD8AEDFF-E24A-4DA1-AD46-4F05D16F33ED
title	Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase (en)
page(s)	wds:Q71816198-67A337B9-8B36-4E6A-8A32-4D4435A2ECAB
page(s)	265-269
instance of	wds:Q71816198-53A9979E-8582-4549-AA75-8959AA57F7D6
instance of	scholarly article
main subject	wds:Q71816198-94C3685F-80E4-432A-891F-D97E377FAEA8
main subject	Escherichia coli
PubMed ID	wds:Q71816198-FE4BF61D-6E28-4B08-AA49-553F7543E461
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7589550
PubMed ID	7589550
published in	wds:Q71816198-8FEA7C18-3569-4752-895D-E646CE5DD04A
published in	FEBS Letters
issue	wds:Q71816198-835C02E8-2554-408C-9E47-A313A238838A
volume	wds:Q71816198-BBD93D79-18CA-4F52-A131-AE88688B49C9
issue	2
volume	374
DOI	wds:Q71816198-F1E2D7FF-54AB-498F-85A5-C097EC5A716D
DOI	http://dx.doi.org/10.1016/0014-5793(95)01125-X
DOI	10.1016/0014-5793(95)01125-X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71816198
is cites work of	One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase Thermodynamics of electron transfer in Escherichia coli cytochrome bo3. Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues. Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis Asymmetric binding of the high-affinity Q(H)(*)(-) ubisemiquinone in quinol oxidase (bo3) from Escherichia coli studied by multifrequency electron paramagnetic resonance spectroscopy. Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 A resolution Elucidating mechanisms in haem copper oxidases: the high-affinity QH binding site in quinol oxidase as studied by DONUT-HYSCORE spectroscopy and density functional theory. QH•-Ubisemiquinone Radical in thebo3-Type Ubiquinol Oxidase Studied by Pulsed Electron Paramagnetic Resonance and Hyperfine Sublevel Correlation Spectroscopy† Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate. Direct evidence for nitrogen ligation to the high stability semiquinone intermediate in Escherichia coli nitrate reductase A. ENDOR spectroscopic studies of stable semiquinone radicals bound to the Escherichia coli cytochrome bo3 quinol oxidase The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli Exploring by pulsed EPR the electronic structure of ubisemiquinone bound at the QH site of cytochrome bo3 from Escherichia coli with in vivo 13C-labeled methyl and methoxy substituents. Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. Interactions of intermediate semiquinone with surrounding protein residues at the Q(H) site of wild-type and D75H mutant cytochrome bo3 from Escherichia coli Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen Probing the Menasemiquinone Binding Mode to Nitrate Reductase A by Selective 2 H and 15 N Labeling, HYSCORE Spectroscopy, and DFT Modeling. Q-Band Electron-Nuclear Double Resonance Reveals Out-of-Plane Hydrogen Bonds Stabilize an Anionic Ubisemiquinone in Cytochrome bo3 from Escherichia coli.
is cites work of	wds:Q54368376-C28073FC-66C7-467D-B550-6BDB866B4266 wds:Q24631329-F11CF416-218F-41EF-B256-8319279B86DB wds:Q54576702-9E2D93D8-E5E8-47C0-A2C7-20824F9CB85A wds:Q36316450-E0A901CE-EBFA-4E7C-8818-364F456C621D wds:Q41633775-9FFE07FA-6434-45F5-997C-3E7334A97BCC wds:Q59457262-A834C295-199F-427E-A640-BA2F2ECF29BE wds:Q34695524-7DA2EBDD-7C14-4F32-8176-28B5D7A664A2 wds:Q36030109-9A5F4F50-42F3-4E47-A509-F5C84185C0FF wds:Q38662205-51195658-251A-4996-BEBF-43EF1850E844 wds:Q39396716-662E9873-88AC-4F16-BB4F-4B54222678E8 wds:Q41821387-FB5D2B9C-1234-4E13-8DA2-B16800C3B131 wds:Q44437412-69CD933F-EECC-47C0-AEB3-3BA41E504160 wds:Q39846772-5A57674C-239C-44F0-B9C3-EEAFEFDB6BE4

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