About: Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.

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About: Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. Goto Sponge NotDistinct Permalink

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scientific article published on February 1996

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1996 (ast) 1996年學術文章 (zh) наукова стаття, опублікована в лютому 1996 (uk) مقالة علمية نشرت في فبراير 1996 (ar) scientific article published on February 1996 (en)
publication date	wds:Q37719995-DD320344-6BC6-4BDD-97BF-DB06146FD2E1
publication date	1996-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37719995-8592E42E-70B6-462E-A584-0C20CE3605BC
language of work or name	English
cites work	wds:Q37719995-1A14D161-931C-4181-9CEA-3F29B107194F wds:Q37719995-244D4B73-60F3-425C-9BF0-9AE0835B28C2 wds:Q37719995-2F210C74-29DC-434D-81E8-0E1198C0D207 wds:Q37719995-45CE9DCC-ADE7-4034-9FD1-B4FABD966462 wds:Q37719995-484D8450-38B0-45C3-BE90-6597175FEFCA wds:Q37719995-6652447D-5707-4CE8-A6A8-1E965D86A1F3 wds:Q37719995-7123D95B-20DE-4737-BF5E-0B293D3204F7 wds:Q37719995-77B9B805-AB53-44D4-BCF7-1D1EA1BAEB82 wds:Q37719995-7971DB27-9ED8-4D85-8D4C-AB7F8635FE6A wds:Q37719995-7E957574-F7FF-4761-A5D4-B04C24781D7A wds:Q37719995-7EAB1EE7-146E-419E-9702-6A04E22EB56E wds:Q37719995-97C75AFF-9702-45B1-B957-66A9B27505BF wds:Q37719995-9949AC60-CF5E-431C-B0BA-B44FCC364CCC wds:Q37719995-B948C819-AA82-4548-8613-8CA194067DCF wds:Q37719995-BD5452DA-4920-4F91-9C63-B8D009FA2789 wds:Q37719995-C226FA10-69D8-4566-A748-91BB445F0FB4 wds:Q37719995-C2EF3BF8-CF54-465C-BE40-9E5C05EA9415 wds:Q37719995-C74637F7-FAA9-4143-9122-BEDBEDB4E933 wds:Q37719995-DEBBA4A9-270B-48E7-99B7-F1A25735685C wds:Q37719995-E140BF4A-3D4F-49FB-8036-CBD444CBBA0D wds:Q37719995-E55232D6-9F2A-47AC-84D5-ADB332674365 wds:Q37719995-E68E9FE8-708B-4D49-85EF-591E43133DC0 wds:Q37719995-EABA25A7-D72B-416F-AC0E-4EBBBBBBD02C wds:Q37719995-F941C1F8-33DA-4B40-AA44-4ABD80A06E05
cites work	Appearance of the v(FeIV = O) vibration from a ferryl-oxo intermediate in the cytochrome oxidase/dioxygen reaction Oxygen activation and the conservation of energy in cell respiration Studies on reduced and oxidized coenzyme Q (ubiquinones). II. The determination of oxidation-reduction levels of coenzyme Q in mitochondria, microsomes and plasma by high-performance liquid chromatography The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type. Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase with oxygen. Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra Properties of the two terminal oxidases of Escherichia coli The heme groups of cytochrome o from Escherichia coli Facilitated intramolecular electron transfer in the Escherichia coli bo-type ubiquinol oxidase requires chloride. Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes. Flow-flash study of the reaction between cytochrome bo and oxygen Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen Molecular cloning, sequencing, and physiological characterization of the qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide Electron and proton transfers through quinones and cytochrome bc complexes Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo Peroxy and ferryl intermediates of the quinol-oxidizing cytochrome aa3 from Bacillus subtilis The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen Electronspin-resonance changes on oxidation of cytochrome oxidase Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli. The reaction of Bacillus subtilis aa3-600 oxidase with oxygen: an aa3-oxidase lacking the CuA site
author name string	wds:Q37719995-1A8AFE2D-06AB-456A-AD3B-269F91467584 wds:Q37719995-22CFEBBE-B3A5-47C1-844F-99FE7AA4DAF5 wds:Q37719995-9DCF2706-F9C8-43AD-BBE0-065BC2CCD302 wds:Q37719995-EA4C324E-02D1-4A17-9A4D-27BCF8DD6D49
author name string	J E Morgan M I Verkhovsky M Wikstrom N P Belevich
rdfs:label	Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (en) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (nl) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (ast)
skos:prefLabel	Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (en) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (nl) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (ast)
name	Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (en) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (nl) Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. (ast)
author	wds:Q37719995-71405077-D7F9-4F6E-AB75-416EF24F3636
author	Anne Puustinen
title	wds:Q37719995-258F0288-B660-40D0-AA8D-BCFC9C441276
title	Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule (en)
page(s)	wds:Q37719995-066DB955-836B-4B08-B74D-7416CFA81952
page(s)	1545-1548
instance of	wds:Q37719995-6349BD97-E391-4163-A6B2-FA37CDBCC06B
instance of	scholarly article
main subject	wds:Q37719995-533408B6-6674-4EA9-8634-BDC65323ADAD
main subject	Escherichia coli
PubMed ID	wds:Q37719995-3255657D-5BCB-493C-9680-1FC03EF31F90
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8643669
PubMed ID	8643669

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