About: Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form

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About: Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 1988

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1988 (uk) im April 1988 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 1988 (ast) scientific article published on 01 April 1988 (en)
publication date	wds:Q68133889-CF5164A8-2D04-48D2-AFA7-05E0D8140319
publication date	1988-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68133889-EE78AD31-05DF-453A-B952-42D3BDD8A4E0
language of work or name	English
cites work	wds:Q68133889-2BBD8BCE-E051-4CE0-B498-2110CE2978E4 wds:Q68133889-3AA7E533-FCE2-4410-BA45-47C664C7E02E wds:Q68133889-3EBAB2EE-8BE2-478E-B282-8D1E49A7E0FF wds:Q68133889-3F91402F-E829-499A-A209-8A4B580B06E9 wds:Q68133889-7A14C588-5B50-4C29-9D53-881CB365DBB2 wds:Q68133889-853022F8-6A6C-4145-B62D-978BB76A1BC3 wds:Q68133889-CADD482B-4E17-43FA-A363-F8A08272CA7E wds:Q68133889-D097069C-6776-4014-A3F8-7BB1655579C3 wds:Q68133889-EF9BAF06-5B14-413C-B9D6-A891D21E7915 wds:Q68133889-F26A61AA-6548-465A-8512-481AE26533F7 wds:Q68133889-F3B40B3D-904F-45AB-898B-AF9322BF0261
cites work	Reactive oxygen intermediates in biochemistry Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli. Proposal that the function of the membrane-bound cytochrome a1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d. Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins Cytochrome c oxidase binding of hydrogen peroxide Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595. Formation and reduction of a ‘peroxy’ intermediate of cytochrome c oxidase by hydrogen peroxide The respiratory chain of Azotobacter vinelandii. I. Spectral properites of cytochrome d The oxidation of cytochrome c oxidase by hydrogen peroxide Effect of ligands on cytochromed fromAzotobacter vinelandii The respiratory chain of Azotobacter vinelandii. II. The effect of cyanide on cytochrome d
author name string	wds:Q68133889-CEFDB4F5-AEE4-4E36-8C0F-F941BAE6A15C
author name string	Poole RK
rdfs:label	Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (en) Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (nl)
skos:prefLabel	Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (en) Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (nl)
name	Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (en) Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (nl)
author	wds:Q68133889-ECB86AB0-E846-4955-8779-63F8B0F047AC
author	Huw D Williams
title	wds:Q68133889-A4D43CC4-9D59-4462-8494-5C87F811F020
title	Formation of the 680 nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form (en)
page(s)	wds:Q68133889-159D6F56-8C0B-4E6C-AB0C-03A4607E87EA
page(s)	243-246
instance of	wds:Q68133889-B55E0475-1619-4459-A1C6-E0243E0CDE01
instance of	scholarly article
main subject	wds:Q68133889-CCB548A0-0F88-4AFC-A625-400594BB8D29
main subject	Escherichia coli
PubMed ID	wds:Q68133889-D17321C6-8A06-4553-9AA5-687C0CCD657B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3282921
PubMed ID	3282921
published in	wds:Q68133889-D7786599-F259-4DAF-A6F0-134C84B07E79
published in	FEBS Letters
issue	wds:Q68133889-018FD224-DE50-4E30-A1AD-A6FD9E1D18E5
volume	wds:Q68133889-F767741A-9195-43EB-9D0A-34A059114A38
issue	1
volume	231
DOI	wds:Q68133889-A06AFADE-9994-492A-B12D-4EAA159A88C1
DOI	http://dx.doi.org/10.1016/0014-5793(88)80740-3
DOI	10.1016/0014-5793(88)80740-3
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68133889
is cites work of	Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation The cytochrome bd respiratory oxygen reductases Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation Cytochrome bd terminal oxidase Gene structure and quinol oxidase activity of a cytochrome bd-type oxidase from Bacillus stearothermophilus Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site. The two terminal oxidases of the aerobic respiratory chain of Escherichia coli each yield water and not peroxide as a final product
is cites work of	wds:Q33977184-15732A8C-68DC-4AD9-994A-50FFF321BBF9 wds:Q40577901-E3524167-97AA-4B5F-BA0D-7E9A014F9C4C wds:Q41613753-B2C555DA-BAFB-40F7-95FB-48EE10896BEA wds:Q35209505-4D01D6C9-BF9E-4E6E-A393-913DADF44FE3 wds:Q54608620-60B8FB4E-97D8-47F1-9174-9B3325CEC9FA wds:Q43026397-5C8D554C-4A59-41A7-BA4C-0864D165E1E3 wds:Q44020359-38B766BF-A374-4847-9737-9CFE01A8933B

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