About: Active site structures of deoxyhemerythrin and oxyhemerythrin

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scientific article published on February 1985

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1985 (ast) наукова стаття, опублікована в лютому 1985 (uk) 1985年學術文章 (zh) مقالة علمية نشرت في فبراير 1985 (ar) scientific article published on February 1985 (en)
publication date	wds:Q37676438-ECE68E44-AC0A-4020-AEE4-200D89A0EEC1
publication date	1985-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37676438-24889156-54E8-4070-A202-CDA8757ECD89
language of work or name	English
cites work	wds:Q37676438-0122FE12-1008-4843-AE24-9BB2D117808B wds:Q37676438-41A3F57E-76EE-43BD-82C6-7795E791B954 wds:Q37676438-5F3986F6-0163-4F08-869B-3A34E833C3C6 wds:Q37676438-657F3DF2-8D46-4D57-981D-A1E68E1543EF wds:Q37676438-67AA62CD-138C-4085-8957-D1228F361A71 wds:Q37676438-81DA626E-B3EE-4184-A33A-3628FB513F1B wds:Q37676438-A6EC5817-70CB-4D98-B332-B1C59F9B9F3E wds:Q37676438-B937CF63-AFE9-461D-B4C6-4EF461314C55 wds:Q37676438-C39C4A1D-7F6B-4C48-8AFA-7A38F347B450 wds:Q37676438-D95D1AD3-3F64-47C4-B6EB-64362AE8C9E2 wds:Q37676438-E277D5CA-A3EB-41D6-800C-48FED3E7178A
cites work	The nature of the active site of hemerythrin Comparison of hemerythrins from four species of sipunculids by optical absorption, circular dichroism, fluorescence emission, and resonance Raman spectroscopy Spectroscopy and structure of hemerythrin Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobin Magnetic susceptibility study of hemerythrin using an ultrasensitive magnetometer Elucidation of the mode of binding of oxygen to iron in oxyhemoglobin by in frared spectroscopy. The state of iron in hemerythrin. A Mössbauer study Active site of hemerythrin. Iron electronic states and the binding of oxygen. Kinetics of the hemerythrin-oxygen interaction Crystallographic studies of azide, thiocyanate and perchlorate complexes of methemerythrin
author name string	wds:Q37676438-103BF00A-12F4-4C43-946D-C6EDBB0CF29D wds:Q37676438-23D637E7-7DB3-4BB5-ACAA-BAFF3ED78287 wds:Q37676438-AA308F7D-C707-4256-BAB1-7606B4FFFFB5 wds:Q37676438-EB59189A-B9F4-4D81-8022-6DC4323D8C5A wds:Q37676438-EDBE4625-C3EC-4D92-834A-F209AE410974
author name string	L C Sieker J Sanders-Loehr R E Stenkamp L H Jensen J D McCallum
rdfs:label	Active site structures of deoxyhemerythrin and oxyhemerythrin (en) Active site structures of deoxyhemerythrin and oxyhemerythrin (nl) Active site structures of deoxyhemerythrin and oxyhemerythrin (ast)
skos:prefLabel	Active site structures of deoxyhemerythrin and oxyhemerythrin (en) Active site structures of deoxyhemerythrin and oxyhemerythrin (nl) Active site structures of deoxyhemerythrin and oxyhemerythrin (ast)
name	Active site structures of deoxyhemerythrin and oxyhemerythrin (en) Active site structures of deoxyhemerythrin and oxyhemerythrin (nl) Active site structures of deoxyhemerythrin and oxyhemerythrin (ast)
title	wds:Q37676438-D0E8DC48-4939-46DE-8A9F-D91CDF20C0C1
title	Active site structures of deoxyhemerythrin and oxyhemerythrin (en)
page(s)	wds:Q37676438-3C7FE724-B5A9-4E7B-83F1-DE524933C6FD
page(s)	713-716
instance of	wds:Q37676438-D74FC284-4065-4722-8AEE-7D4768E48AA9
instance of	scholarly article
PubMed ID	wds:Q37676438-D71248F8-EFDE-4FCD-A52A-FDF734A7C8A9
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3856224
PubMed ID	3856224
published in	wds:Q37676438-77554015-A986-4079-A88C-90EF3E58F27C
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37676438-B69128C6-3CDF-4883-94D9-D5922160289A
volume	wds:Q37676438-28776E60-94EF-4F01-8737-92D203D7B803
issue	3
volume	82
DOI	wds:Q37676438-486FEDD2-7471-4918-85A2-41ECFFE8F934
DOI	http://dx.doi.org/10.1073/PNAS.82.3.713
DOI	10.1073/PNAS.82.3.713
ResearchGate publication ID	wds:Q37676438-F52EFCC9-405F-4CCA-A0C8-F33EA28B2033
ResearchGate publication ID	19306163
ADS bibcode	wds:Q37676438-C7CBDBF4-B3C7-4144-8181-A4D054D5EF9F
ADS bibcode	1985PNAS...82..713S
PMCID	wds:Q37676438-72AFBF28-0115-4AA6-B0AC-1EE90B5CF5FB
PMCID	397116
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37676438
is cites work of	Three-dimensional structure of the free radical protein of ribonucleotide reductase Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O2 activation mechanism. Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry Redox and acid-base properties of asymmetric non-heme (hydr)oxo-bridged diiron complexes. Mechanisms of cooperativity and allosteric regulation in proteins Water oxidation chemistry of photosystem II. Getting a sense for signals: regulation of the plant iron deficiency response The bHLH transcription factor POPEYE regulates response to iron deficiency in Arabidopsis roots Cloning and expression analysis of a cDNA that encodes a leech hemerythrin. Oxygen Activation t the Diiron Center of Ribonucleotide Reductase Protein degradation and iron homeostasis Structure, function and evolution of the hemerythrin-like domain superfamily.

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