About: Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Juli 1957 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в липні 1957 (uk)
publication date	wds:Q59096718-0A63B99D-E6E2-4931-A6C6-C64BE2ECCBBF
publication date	1957-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59096718-DB13063A-B981-42A5-B90C-EC3985C708D3
language of work or name	English
exact match	wds:Q59096718-2B4ABB80-F91B-4910-BC96-E1B99F0DBB89
exact match	https://scigraph.springernature.com/pub.10.1038/180030a0
author name string	wds:Q59096718-9621FBA4-2276-461B-A2D0-0487628E484A
author name string	J S GRIFFITH
rdfs:label	Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (en) Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (nl)
skos:prefLabel	Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (en) Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (nl)
name	Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (en) Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide (nl)
title	wds:Q59096718-DD5E632E-BA94-4DAB-A065-F6D4CF1450AC
title	Theory of electron resonance in ferrihaemoglobin azide (en)
page(s)	wds:Q59096718-E17C46F3-91DE-41BD-A766-86F74AE6DF20
page(s)	30-31
instance of	wds:Q59096718-E846398B-48D4-4633-839D-D1B7210641E2
instance of	scholarly article
PubMed ID	wds:Q59096718-62D8F560-F166-43C1-8B53-89474E4D5615
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13451631
PubMed ID	13451631
published in	wds:Q59096718-B8490FDE-8C96-4EDF-9450-CC8D45747EFC
published in	Nature
issue	wds:Q59096718-193061C9-FEF5-40A1-A5FB-00F7D316324D
volume	wds:Q59096718-C219B0DC-B8D3-419B-BD56-C4C05F333480
issue	4575
volume	180
DOI	wds:Q59096718-B811C9F1-7293-4FDC-A72E-2AA7AA22B1A6
DOI	http://dx.doi.org/10.1038/180030A0
DOI	10.1038/180030A0
Dimensions Publication ID	wds:Q59096718-504BDC0E-0F70-4EAF-8AD0-1A45E0CA81C9
Dimensions Publication ID	1045811702
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59096718
is cites work of	Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c Modulation of the ligand-field anisotropy in a series of ferric low-spin cytochrome c mutants derived from Pseudomonas aeruginosa cytochrome c-551 and Nitrosomonas europaea cytochrome c-552: a nuclear magnetic resonance and electron paramagnetic res 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 THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase End-On and Side-On Peroxo Derivatives of Non-Heme Iron Complexes with Pentadentate Ligands: Models for Putative Intermediates in Biological Iron/Dioxygen Chemistry 20 Mössbauer spectroscopy of proteins: Electron carriers Mössbauer effect in some haemoglobin compounds Identification of a low-spin acylperoxoiron(III) intermediate in bio-inspired non-heme iron-catalysed oxidations. Mössbauer spectroscopy of haem proteins Proton Nuclear-Magnetic-Resonance Study of Low-Spin Ferriprotoporphyrin(IX) Dimethyl Ester Electron capture by oxyhaemoglobin: an e. s. r. study Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster Models of the bis-histidine-coordinated ferricytochromes: Mössbauer and EPR spectroscopic studies of low-spin iron(III) tetrapyrroles of various electronic ground states and axial ligand orientations Mössbauer Spectroscopy of Cytochrome c Electron paramagnetic resonance spectra of mitochondrial and microsomal cytochrome P-450 from the rat adrenal The nature of the axial ligands of spinach cytochrome f FEATURES OF THE ELECTRONIC STRUCTURE OF THE IRON-PORPHYRIN COMPLEXES WITH SPECIAL REFERENCE TO THE OXIDO-REDUCTIVE PROPERTIES OF CYTOCHROMES CW-EPR and ENDOR study of cytochrome c6 from Anabaena PCC 7119. Electronic structure of cyanide complexes of hemes and heme proteins Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase Heme proteins and model compounds: Mössbauer absorption and emission spectroscopy Paramagnetic NMR shifts in cyanoferricytochrome c The electronic g-tensor in cytochrome b5: High resolution proton magnetic resonance studies Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy. Soluble and membrane-bound paramagnetic centers inMethanobacterium Bryantii Analysis of the paramagnetic shifts of haem carbon resonances in bovine ferricytochrome b5 Mössbauer Characterization ofParacoccus denitrificansCytochromecPeroxidase Determination of zero-field splitting and evidence for the presence of charge-transfer transitions in the Soret region of high-spin ferric hemoproteins obtained from an analysis of low-temperature magnetic circular dichroism Mössbauer study of cytochrome c2 from Rhodospirillum rubrum Sign of the product gxgygz of some low spin ferric heme proteins Leghemoglobin. An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate Mössbauer study of iron bleomycin and its activation intermediates Proton magnetic resonance studies of porphyrin iron (3) cyanides Electron paramagnetic resonance studies of the purified cytochrome P-450scc and P-45011β from bovine adrenocortical mitochondria Structure and spin density of ferric low-spin heme complexes determined with high-resolution ESEEM experiments at 35 GHz. The photosynthetic cytochrome c 550 from the diatom Phaeodactylum tricornutum. Infrared magnetic circular dichroism of myoglobin derivatives Pulse EPR Methods for Studying Chemical and Biological Samples Containing Transition Metals Characterization of a sulfite reductase from Desulfovibrio vulgaris. Evidence for the presence of a low-spin siroheme and an exchange-coupled siroheme-[4Fe-4S] unit Mössbauer and electron paramagnetic resonance studies of chloroperoxidase following mechanism-based inactivation with allylbenzene Strength of axial water ligation in substrate-free cytochrome P450s is isoform dependent. Correlations among parameters that describe low-spin ferric heme complexes 4 Electron Spin Resonance in Medicinal Chemistry
is cites work of	wds:Q39892194-C7BCC468-0BF6-458E-9BC3-B4BF4AE82578 wds:Q39202240-47BEFFA7-D719-41CC-9C21-C87B680ED54A wds:Q63248607-3A5451C9-95B1-4EAD-901F-B19F083D03FA wds:Q72916260-19172E1A-9A63-4A19-B396-4B5620B4D145 wds:Q71426412-92CF3772-B350-410D-9EB4-88FBB23B49F3 wds:Q77910432-4230695C-F6A1-43C9-9E8C-FA56CE94ECB0 wds:Q39131668-A08F600B-B603-4B7D-B4EC-A8BCA76FB550 wds:Q43090992-CB21969D-2919-4D4B-BC9A-15CAA9A7E15A wds:Q40015304-D50067FD-B260-428A-9258-B7DA94B99C17 wds:Q48110011-39C98099-76B2-41CF-AE1E-DBD1CD65BBCF wds:Q61755427-85E1E9AD-7C3D-4B59-BC36-211AF3A4D9FC wds:Q52702041-9EFC952B-7B8C-4173-AA3A-1A203D67E296 wds:Q37148552-0FEC9BBA-60CB-4290-BA03-7F65219A6738 wds:Q36683807-8F691FBD-53A1-486B-8728-EEB1C3998E47 wds:Q40056273-AC6DDBDC-21CC-428C-9495-372E48AB6222

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