About: Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 March 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 1996 (uk) article scientifique publié en 1996 (fr) im März 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en marzu de 1996 (ast) scientific article published on 01 March 1996 (en)
publication date	wds:Q71069927-988E8070-F6E4-4487-A7FF-78CB1D9660E8
publication date	1996-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71069927-51C1C4FC-19A7-4F6A-BAD6-F0E45CC455FD
language of work or name	English
cites work	wds:Q71069927-019202C7-2D5F-447F-8F5C-50C1B0C8D6DD wds:Q71069927-046A4FDB-7B04-4D0C-9E26-E39EEE4D0275 wds:Q71069927-0DD9D24F-7AD4-4498-884C-C5448EABD2C1 wds:Q71069927-170AC74D-185E-4DCA-907D-88212709F8E9 wds:Q71069927-180C3365-F2DF-4F91-BDFD-2FC430B8C1DD wds:Q71069927-1EC7F052-5B84-41BA-8BFF-E29431313953 wds:Q71069927-2913FCBB-5652-4DF7-B812-FF1AF0C0A1A7 wds:Q71069927-2CE89023-DA4A-4276-8D0F-1B2EFAD55CBC wds:Q71069927-2E01A426-4833-4ACB-963D-5B2528189BCC wds:Q71069927-456C22F9-5914-4297-AFF7-47A5ED270500 wds:Q71069927-47D982AA-A28B-4404-8031-6DAB88B5FE7F wds:Q71069927-4FCE1C80-206D-452E-8238-3E89333A6A3B wds:Q71069927-5018D3A2-F78A-459F-B383-33E6BB149EB2 wds:Q71069927-54ABE508-405A-4D9F-8893-3F947410152D wds:Q71069927-58792A00-14DD-4F4A-A02D-1B127C1339FF wds:Q71069927-58918DCA-A5E6-4763-A9BE-B2954431EED3 wds:Q71069927-657A1CA6-B3D7-4A41-9967-77F995E56BDD wds:Q71069927-6718612A-C53B-4497-8AF8-2AD7D560B2B9 wds:Q71069927-7096B097-9BF8-4308-942C-AC6CCB93CB37 wds:Q71069927-7E42410D-4AB5-49BC-B01D-D9A8ACC7BCD5 wds:Q71069927-95563604-967A-46AA-BF0D-8C7C3307C45F wds:Q71069927-A001CB70-2EBF-40E1-8847-F9F1791B9513 wds:Q71069927-A50354DD-3776-4C0B-946D-8B0C578B3779 wds:Q71069927-A86B96AE-FD39-4786-B20D-A1208537AB64 wds:Q71069927-B8791299-9665-49E4-868F-A615B757750F wds:Q71069927-B97A6E12-524F-4F1C-BE33-48BFDAB5161E wds:Q71069927-C6FADEE1-2D9E-4810-8BFF-12777EB8FCA5 wds:Q71069927-CEA6BA8B-EEA4-4771-B875-F3649E8A8499 wds:Q71069927-D2DE2861-B894-4F51-A67B-BF3A1D0B675F wds:Q71069927-E7393611-B2BF-401E-A272-5A20EABDA44E wds:Q71069927-F0F5A2A8-8AC8-4055-8C73-8CCB5988FA8D wds:Q71069927-F310C471-B74D-4CCF-B7AD-7D99255E7FF2 wds:Q71069927-FB1BC3EB-8F0F-46B9-8EA7-1C29DBF1A4D4 wds:Q71069927-FDE5E0AD-7062-4B42-9D33-6012B2049862
cites work	The mitochondrial electron transport and oxidative phosphorylation system The protonmotive Q cycle: A general formulation Studies on the electron-transport system. 27. The respiratory activity of acetoneextracted beef-heart mitochondria: role of coenzyme Q and other lipids Protonmotive redox mechanism of the cytochrome b-c 1 complex in the respiratory chain: Protonmotive ubiquinone cycle The protonmotive Q cycle in mitochondria and bacteria. Function of the iron-sulfur protein of the cytochrome b-c1 segment in electron-transfer and energy-conserving reactions of the mitochondrial respiratory chain Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: cytochrome c oxidoreductase? Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model Use of specific inhibitors on the mitochondrial bc1 complex The bc1 complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus Possible molecular mechanisms of the protonmotive function of cytochrome systems Properties of a semiquinone anion located in the QH2:cytochrome c oxidoreductase segment of the mitochondrial respiratory chain Changes in oxidation-reduction potential of cytochrome b observed in the presence of antimycin A Studies with ubiquinone-depleted submitochondrial particles. Essentiality of ubiquinone for the interaction of succinate dehydrogenase, NADH dehydrogenase, and cytochrome b Reconstitution of the electron transport system. I. Preparation and properties of the interacting enzyme complexes A proposed pathway of proton translocation through the bc complexes of mitochondria and chloroplasts Evidence for the existence of a ubiquinone protein and its radical in the cytochromes and region in the mitochondrial electron transport chain Identification of ubiquinone-binding proteins in yeast mitochondrial ubiquinol-cytochrome c reductase using an azido-ubiquinone derivative The restoration of DPNH oxidase activity by coenzyme Q (ubiquinone). Large-scale purification and characterization of a highly active four-subunit cytochrome bc1 complex from Rhodobacter sphaeroides Essentiality of the molecular weight 15,000 protein (subunit IV) in the cytochrome b-c1 complex of Rhodobacter sphaeroides Rhodobacter capsulatus mutants lacking the Rieske iron sulfur protein form a stable cytochrome bc1 subcomplex with an intact quinone reduction site The role of phospholipids in the binding of antimycin to yeast Complex III Kinetics of cytochrome b oxidation in antimycin-treated submitochondrial particles EPR characterization of the cytochrome b-c1 complex from Rhodobacter sphaeroides On the oxidation pathways of the mitochondrial bc1 complex from beef heart. Effects of various inhibitors The small molecular mass ubiquinone-binding protein (QPc-9.5 kDa) in mitochondrial ubiquinol-cytochrome c reductase: isolation, ubiquinone-binding domain, and immunoinhibition Coenzyme Q analogues reconstitute electron transport and proton ejection but not the antimycin-induced "red shift" in mitochondria from coenzyme Q deficient mutants of the yeast Saccharomyces cerevisiae The oxidation of ubiquinol by the isolated Rieske iron-sulfur protein in solution Studies on the function and biogenesis of cytochrome b in mutants of Saccharomyces cerevisiae resistant to 3-(3,4-dichlorophenyl)-1,1-dimethylurea Subunit analysis of bovine cytochrome bc1 by reverse-phase HPLC and determination of the subunit molecular masses by electrospray ionization mass spectrometry Reduction of cytochrome b in mitochondria from yeast lacking coenzyme Q. Studies on the electron transport system. XXIII. Coenzyme Q oxidase
author name string	wds:Q71069927-3E776C7C-290E-4741-A073-0A8D7356CC9A wds:Q71069927-CF13D745-88E7-4AC4-B47C-8C88120084FD
author name string	A Matsuno-Yagi Y Hatefi
rdfs:label	Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (en) Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (nl)
skos:prefLabel	Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (en) Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (nl)
name	Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (en) Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (nl)
title	wds:Q71069927-75591A37-910C-4263-B10A-007C2608FBB3
title	Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems (en)
page(s)	wds:Q71069927-3AD6865E-AD82-45D4-96D3-8C7A59DADA22
page(s)	6164-6171
instance of	wds:Q71069927-7A2BB2CC-F976-4BE4-AB80-296D029F964A
instance of	scholarly article
PubMed ID	wds:Q71069927-3D8BC613-78BA-400F-85B1-73F97D30CD22
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8626405
PubMed ID	8626405
published in	wds:Q71069927-7E785CF8-DDDD-42C0-9143-535F5251DFF9
published in	Journal of Biological Chemistry

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software