About: Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3

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About: Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 Goto Sponge NotDistinct Permalink

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Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття (uk)
publication date	wds:Q95349653-F778EAE7-4892-41D7-AFF7-3B5EC7B75EAA
publication date	1971-06-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q95349653-89F9E9EE-401D-47D8-A6D6-1BCF50FFDB5C wds:Q95349653-A4B9A4C8-6949-4587-B21F-A335D431CCF1
author name string	B F van Gelder M F Blokzijl-Homan
rdfs:label	Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (en) Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (nl)
skos:prefLabel	Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (en) Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (nl)
name	Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (en) Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (nl)
title	wds:Q95349653-951245F0-11B3-4BCD-89B5-541171B9BB00
title	Biochemical and biophysical studies on cytochrome aa 3 . 3. The EPR spectrum of NO-ferrocytochrome a 3 (en)
page(s)	wds:Q95349653-0AF23AEF-2E43-4354-B460-4053D6AEFC08
page(s)	493-498
instance of	wds:Q95349653-4D3829FA-E89D-45EF-9E4E-BCC96BE5E73C
instance of	scholarly article
PubMed ID	wds:Q95349653-4C2197D8-98FE-4883-9B75-76588B2FA9AA
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4330152
PubMed ID	4330152
published in	wds:Q95349653-3CBBA00C-E632-401E-B752-5C2CA99A836B
published in	Biochimica et Biophysica Acta
issue	wds:Q95349653-95A42997-7A87-49B7-8921-E21B8411975E
volume	wds:Q95349653-41F74C4A-C5B7-4E96-8596-7D34BF82272D
issue	3
volume	234
DOI	wds:Q95349653-3C74914F-E609-44F3-98DE-ADA31CA990C3
DOI	http://dx.doi.org/10.1016/0005-2728(71)90215-5
DOI	10.1016/0005-2728(71)90215-5
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q95349653
is cites work of	Structural models of the redox centres in cytochrome oxidase Fourier transform infrared characterization of a CuB-nitrosyl complex in cytochrome ba3 from Thermus thermophilus: relevance to NO reductase activity in heme-copper terminal oxidases. Calcium-Independent Modulation of Cyclic GMP and Activation of Guanylate Cyclase by Nitrosamines Electron paramagnetic resonance- (EPR-) resolved kinetics of cryogenic nitric oxide recombination to cytochrome c oxidase and myoglobin. Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide? Activation of cerebral guanylate cyclase by nitric oxide Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen-binding site Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies Low-spin ferric forms of cytochrome a3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase Nitric oxide, a biological effector. Electron paramagnetic resonance detection of nitrosyl-iron-protein complexes in whole cells. Nitric oxide and mitochondrial respiration Reactivity of nitric oxide with cytochrome c oxidase: interactions with the binuclear centre and mechanism of inhibition. Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures A model for cytochrome oxidase The interaction between heme and protein in cytochrome c1 Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector? Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide Electron paramagnetic resonance studies on Pseudomonas nitrosyl nitrite reductase. Evidence for multiple species in the electron paramagnetic resonance spectra of nitrosyl haemoproteins Electron paramagnetic resonance studies of nitrosyl ferrous heme complexes. Determination of an equilibrium between two conformations Direct electron transfer to cytochrome c oxidase in self-assembled monolayers on gold electrodes Electron-Spin Resonance of Nitrosyl Haemoglobins: Normal alpha and beta Chains and Mutants Hb M Iwate and Hb Zurich 21 Ligands of cytochrome c oxidase Electron nuclear double resonance and electron paramagnetic resonance study on the structure of the NO-ligated heme alpha 3 in cytochrome c oxidase EPR studies of the photodissociation reactions of cytochrome c oxidase-nitric oxide complexes Reactions of mercaptans with cytochrome c oxidase and cytochrome c Orientation of the NO ligand of cytochrome a3in nitrosyl cytochrome c oxidase Nitric oxide inhalation therapy for newborn infants EPR studies of15NO-ferrocytochromea3in cytochromecoxidase Hydrazine and hydroxylamine as probes for O2-reduction site of mitochondrial cytochrome c oxidase. Butylhydroxylamine inhibits H+ -driven atp synthesis of the TF1 · FO -ATPase incorporated into liposomes Proton nuclear magnetic resonance study of bovine cytochrome oxidase Angular dependence of electron paramagnetic resonances of an azide-NO complex of cytochrome c oxidase: orientation of the haem-copper axis in cytochrome aa3 from ox heart The effects of copper depletion on structural aspects of cytochrome c oxidase
is cites work of	wds:Q34498075-C28BC700-6F55-440E-85A9-D609A01A67A1 wds:Q39147309-C0528E13-96CC-4BFB-84B5-104803A7E933 wds:Q39105176-968409D4-6202-4F06-AD1C-D748F038341B wds:Q52704729-8F3F057F-BF53-4800-8A6F-93B439CFF16E wds:Q59162718-65764D32-1627-44CD-A5C3-7F7B60B45CB7 wds:Q70211637-A318710A-89D8-4A29-B0BC-31774833374A wds:Q30428889-7C98A859-7216-49EB-8BB3-5833D27F5376 wds:Q47983341-772D9D98-E8C5-4E42-9759-B2E56901ED4C wds:Q72758630-04E21623-B9FA-4344-903D-8F2D27EA4756 wds:Q73744784-09C249B1-A3D6-446A-A613-D9CAE82F6462 wds:Q24556092-A095881D-541F-4A9A-A838-73A51140D2BF wds:Q33631341-F842D7EB-B5B3-4B5F-90D7-32FD4D586FFD wds:Q36436856-AD8AEFFA-A92D-4140-BB07-0F4080DE6980 wds:Q40203759-4C287B7B-CA62-4693-B06F-1913CCA5A534 wds:Q42147739-46A8A913-6B02-4C85-A302-0E6160193E15 wds:Q74469842-08174F0A-C9B5-4EA6-A793-77C7BC237984 wds:Q70157933-B3914DB6-8CAE-42D0-82C1-F5423ACD193F wds:Q40216764-7D1E20D4-106D-49C7-859A-D5DA1B6609AF wds:Q40185452-5A187799-AF4D-4A05-B56C-6B14DEDD737A wds:Q50934044-5DCC3EF6-FEE1-4990-AD05-0B6D20EF6807 wds:Q72919830-8918C8E8-6A33-45F0-8ADB-B29F3A18D439 wds:Q72920688-6742971D-B11D-47C0-9D4A-531292FA5480 wds:Q37116990-AD9EFE6F-D521-4095-865A-52AFA6EF970A wds:Q37336559-32967ABC-1A44-4EBA-B3CE-60E6D6D7F862 wds:Q41843280-71D7CA1D-217D-4295-8D84-BB147E2031FD wds:Q41898728-A690317A-9382-4726-ABF2-C00AD782A6FE wds:Q67264250-3511904E-4758-465D-9869-6F7E8D69C46D wds:Q72844154-1E8A98DC-8C33-48E6-99B3-082C1761BE44 wds:Q34534568-3DCBE81C-6974-4AED-9B75-C9068F86BF86 wds:Q35007823-5F4CF3BD-FA52-4465-BF01-0CA2442934AC wds:Q42282146-285852AC-6F24-425C-B7A3-290F15EC73AC wds:Q36901765-028A0B2D-149C-49B1-ADD0-8A8D64BB8B0F

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