About: Electron paramagnetic resonance of beef-heart ferricytochrome c

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scientific article published on 01 March 1968

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 1968 (uk) im März 1968 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en marzu de 1968 (ast) scientific article published on 01 March 1968 (en)
publication date	wds:Q68577738-2AD521C1-B9BB-45F6-8364-D18906AD2CE8
publication date	1968-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68577738-C2DDD216-B3B9-4B67-A13D-DABBB27B8D5B
language of work or name	English
cites work	wds:Q68577738-39399557-6CAF-416F-ACE0-DA7058BCA44A wds:Q68577738-48CD349C-1502-41BF-ACFD-08A8008AC562 wds:Q68577738-B5F80807-4773-4DF1-BA70-5CE574F9AD3A
cites work	Electronic spectrum of single crystals of ferricytochrome-c On the compounds of ferricytochrome c appearing in acid solution Crystal Spectra of a Heme and Some Heme-Protein Complexes*
author name string	wds:Q68577738-2F119968-F253-4D53-AD5C-A5CA09F37E26 wds:Q68577738-33844410-93D6-432E-9F3A-B5AF584583E6
author name string	G Palmer I Salmeen
rdfs:label	Electron paramagnetic resonance of beef-heart ferricytochrome c (en) Electron paramagnetic resonance of beef-heart ferricytochrome c (nl)
skos:prefLabel	Electron paramagnetic resonance of beef-heart ferricytochrome c (en) Electron paramagnetic resonance of beef-heart ferricytochrome c (nl)
name	Electron paramagnetic resonance of beef-heart ferricytochrome c (en) Electron paramagnetic resonance of beef-heart ferricytochrome c (nl)
title	wds:Q68577738-9099CFC6-21C4-4612-93CF-54BCF15A00FF
title	Electron paramagnetic resonance of beef-heart ferricytochrome c (en)
page(s)	wds:Q68577738-B00EACC8-CF46-404B-ACD9-1BB1BDC37BAD
page(s)	2049-2052
instance of	wds:Q68577738-09873B55-D1A5-4B51-A584-4AD74AB72140
instance of	scholarly article
PubMed ID	wds:Q68577738-4038A839-6113-42DC-BCF6-DA5363CD4B91
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4297179
PubMed ID	4297179
published in	wds:Q68577738-DE4E9C49-795E-4A1C-A684-ABD024B9D931
published in	Journal of Chemical Physics
issue	wds:Q68577738-86B8AC4D-3AC2-48ED-BACA-E3D7DD597281
volume	wds:Q68577738-E9CBD486-7ED8-40AA-948C-AADA974BCCFB
issue	5
volume	48
DOI	wds:Q68577738-347B9A7A-71EB-4FF2-84AE-6699D675C76D
DOI	http://dx.doi.org/10.1063/1.1669014
DOI	10.1063/1.1669014
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68577738
is cites work of	Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c Resonance Raman Spectra of Hemoglobin and Cytochrome c: Inverse Polarization and Vibronic Scattering Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands. Spin state and ligand affinity comparison to myoglobin The primary electron acceptor in photosynthesis Axial coordination of heme in ferric CcmE chaperone characterized by EPR spectroscopy Single‐Crystal Spectra of Ferrimyoglobin Complexes in Polarized Light Time-resolved resonance Raman spectroscopy of cytochrome c reduced by pulse radiolysis The EPR of low spin heme complexes Relation of the τ2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters Electron paramagnetic resonance study of the high- and low-spin forms of cytochrome P-450 in liver and in liver microsomes from a methylcholanthrene-treated rabbit Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8 Mössbauer spectroscopy of haem proteins Studies on the heme environment of horse heart ferric cytochrome c azide and imidazole complexes of ferric cytochrome c 11 EPR spectroscopy of components of the mitochondrial electron-transfer system Mössbauer studies of the iron atom in cytochrome c Electron spin relaxation of the electron paramagnetic resonance spectra of cytochrome c A comparison of the physical and chemical properties of four cytochromes c from Azotobacter vinelandii Double Nuclear Magnetic Resonance Observation of Electron Exchange between Ferri- and Ferrocytochrome c EPR signals from cytochrome c oxidase Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c Influence of light on the EPR-detectable, electron transport components in whole cell Rhodospirillum rubrum Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase Interactions of the major metabolite of the cancer chemopreventive drug oltipraz with cytochrome c: a novel pathway for cancer chemoprevention The electronic g-tensor in cytochrome b5: High resolution proton magnetic resonance studies The binding characteristics of the cytochrome c iron The spin 3/2 state and quantum spin mixtures in haem proteins Mitochondrial respiratory chain of Tetrahymena pyriformis The properties of submitochondrial particles and the soluble b and c type pigments EPR studies of protein state transitions in Chromatium ferricytochrome ′ Cytochrome c-554 from Methylosinus trichosporium OB3b; a protein that belongs to the cytochrome c2 family and exhibits a HALS-Type EPR signal Near-infrared absorption and circular dichroism spectra of ferrocytochrome c: d-d transitions Modified cytochrome c/H2O2 system: spectroscopic EPR investigation of the biocatalytic behaviour The novel “g' = 1.74” EPR spectrum of pink and purple uteroferrin Correlations among parameters that describe low-spin ferric heme complexes Application of a superconducting susceptometer to biological samples Solubilisation of ferricytochrome c in methanol using a crown ether: absorption, circular dichroism and EPR spectral properties Measurement of the spin concentration of metalloprotein samples from saturation-magnetization data with particular reference to cytochrome c oxidase
is cites work of	wds:Q33702330-9E2F88AB-A8D3-447D-A8BA-E6D7AC831BBD wds:Q34729159-95238050-28C9-450F-8DBE-D6E936BDAE44 wds:Q40199842-52FE3C0F-8C38-4413-A244-73237F62C262 wds:Q39892194-5A91DF61-DD4F-4E66-BE2B-D6C5DDD8D98E wds:Q39131668-9ADC576E-55FE-481F-BD48-B66367F0E174 wds:Q72110679-3C7019EF-EA6A-487A-BB6D-088E28415880 wds:Q37103355-AE397C92-3F9A-4FE2-A4C3-6B69E4FFF8D2 wds:Q40056273-2B7CD6E0-C1E6-44E5-9806-7305C363BD2D wds:Q42818399-424FB10A-6E78-4195-A962-83434ACFF720 wds:Q52766399-90AAFE3F-A7BD-47E4-B09F-F155424EB2A2 wds:Q72926577-0E21798A-5766-4532-89F4-4BC7012716C5 wds:Q33815474-58A36F38-8061-4AE1-A800-CECF39DBF616 wds:Q39941472-60172D33-84CF-48CB-8429-E9022DFF5DB3 wds:Q72908094-59013A6B-41C2-427F-AC0F-1B3A8F0FB322 wds:Q36350561-7756297D-D5EE-47D3-AE32-8919E4CEDAEB wds:Q40122181-61FC8CDD-B142-40EF-8961-C9B89F294A44 wds:Q41332817-D76393C2-ADC7-4994-A092-8277F600D2F4 wds:Q72395944-8901CD8C-40BA-42A3-A04A-F05F9141725B wds:Q60190835-3AA1AFE9-E8B8-4590-93AE-3D1A20057D40 wds:Q71521098-C5362816-9B69-42F2-ABCE-E31C8F440692

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