About: Heme orientational disorder in reconstituted and native sperm whale myoglobin

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About: Heme orientational disorder in reconstituted and native sperm whale myoglobin Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1983

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1983 (uk) article scientifique publié en 1983 (fr) im August 1983 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'agostu de 1983 (ast) scientific article published on 01 August 1983 (en)
publication date	wds:Q57972926-A6F6D107-F6AD-4EBE-B7A5-FD58D797EFEA
publication date	1983-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57972926-9841CD50-F7D6-4E1A-A5A0-2FA00E2C4137
language of work or name	English
cites work	wds:Q57972926-0362A0B0-B519-41F1-990C-AE6B6B22C6A6 wds:Q57972926-077A1C92-AD7D-496F-A68D-1361709F2BEF wds:Q57972926-2F1032FB-8547-4A39-B4AB-C07A44DC4ED2 wds:Q57972926-6576F201-4189-496F-9E46-ECA7FE68EE7D wds:Q57972926-677EFD47-154C-4243-B27B-D03E04CE27BF wds:Q57972926-8FDC3B7B-0B78-452F-96D5-416D0CF32D80 wds:Q57972926-95AB2381-6583-4B57-996C-17919CFE0010 wds:Q57972926-9A3C32FE-53C4-48B1-92E2-C24968BD0894 wds:Q57972926-A2EF4AB5-2164-475C-AA13-81694EB46541 wds:Q57972926-A528636B-8B3C-4EE4-A2EB-3EF0EAA4575D wds:Q57972926-C208EA92-7677-4C11-AFB9-6C784F74DC7A wds:Q57972926-C97CAF96-798C-4AE1-87F0-80FFE336945D wds:Q57972926-D0B96852-89A2-45DB-9754-E3E6B7B47A90 wds:Q57972926-E879E823-6C92-446B-B7C5-21B467A8E1F2 wds:Q57972926-FCFABDB2-55CE-4614-BD80-7631C8F42FC9
cites work	Acid Bohr effects in myoglobin characterized by proton NMR hyperfine shifts and oxygen binding studies Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution Structure and refinement of oxymyoglobin at 1.6 A resolution Cleavage of the haem-protein link by acid methylethylketone Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale Pyrroles and related compounds. Part XXXIII. Total synthesis of deuteriated derivatives of protoporphyrin-IX for nuclear magnetic resonance studies of haemoproteins Neutron Diffraction Analysis of Myoglobin: Structure of the Carbon Monoxide Derivative Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuteration Properties of Components of Myoglobin of the Sperm Whale Electronic structure of cyanide complexes of hemes and heme proteins Assignment of hyperfine-shifted resonances in low-spin forms of cytochrome c peroxidase by reconstitutions with deuterated hemins Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins New syntheses of deuterated protoporphyrin-IX derivatives for heme protein nmr studies Proton nuclear magnetic resonance investigation of the nature of solution conformational equilibria of monomeric insect deoxyhemoglobins.
author name string	wds:Q57972926-B2A6E398-9486-41EB-B3E1-D6F655C1F504 wds:Q57972926-BA396BDE-943D-4761-8A51-949FBF360BE8 wds:Q57972926-FBBD4DA0-C3D9-4508-B969-CD76B439F5D2
author name string	G N La Mar N L Davis D W Parish
rdfs:label	Heme orientational disorder in reconstituted and native sperm whale myoglobin (en) Heme orientational disorder in reconstituted and native sperm whale myoglobin (nl)
skos:prefLabel	Heme orientational disorder in reconstituted and native sperm whale myoglobin (en) Heme orientational disorder in reconstituted and native sperm whale myoglobin (nl)
name	Heme orientational disorder in reconstituted and native sperm whale myoglobin (en) Heme orientational disorder in reconstituted and native sperm whale myoglobin (nl)
author	wds:Q57972926-8D1082EA-2985-46BE-A53D-24A1E6994F26
author	Kevin M. Smith
title	wds:Q57972926-EE0F6173-7A1D-4A2B-8CE3-26892399EC05
title	Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein (en)
page(s)	wds:Q57972926-71F02D21-E751-4CC4-AEA5-D5746D3E3EC7
page(s)	887-896
instance of	wds:Q57972926-C16C665C-62FF-4B5F-A690-6751FBAF59AF
instance of	scholarly article
PubMed ID	wds:Q57972926-D7087CDA-A96F-4F15-AE09-E55EA19B7935
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6887254
PubMed ID	6887254
published in	wds:Q57972926-4174EEC8-DEAB-4C08-957D-79CFEEE6B6A1
published in	Journal of Molecular Biology
issue	wds:Q57972926-8B667F71-02C3-4DA9-A62A-5565A70F353B
volume	wds:Q57972926-915EE64D-D171-4ACB-B636-66EB4BFA2002
issue	4
volume	168
DOI	wds:Q57972926-EBB54CCA-46A8-4697-902D-C205848853AA
DOI	http://dx.doi.org/10.1016/S0022-2836(83)80080-1
DOI	10.1016/S0022-2836(83)80080-1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57972926
is cites work of	Effects of pH on the kinetic reaction mechanism of myoglobin unfolding studied by time-resolved electrospray ionization mass spectrometry. Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering Assembly of human hemoglobin. Studies with Escherichia coli-expressed alpha-globin. Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli. Recombinant human hemoglobin: expression and refolding of beta-globin from Escherichia coli Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: stability, structure, and dynamics of axial ligand complexes Still a puzzle: why is haem covalently attached in c-type cytochromes? Haem disorder in recombinant- and reticulocyte-derived haemoglobins: evidence for stereoselective haem insertion in eukaryotes Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy Charge-Disproportionation Symmetry Breaking Creates a Heterodimeric Myoglobin Complex with Enhanced Affinity and Rapid Intracomplex Electron Transfer Heme-protein interactions in horse heart myoglobin at neutral pH and exposed to acid investigated by time-resolved fluorescence in the pico- to nanosecond time range Heme orientation affects holo-myoglobin folding and unfolding kinetics 1 Haem disorder in two myoglobins: comparison of reorientation rate Characterization of haem disorder by circular dichroism Detection of myoglobin desaturation in Mirounga angustirostris during apnea Kinetics of the reconstitution of hemoglobin from semihemoglobins alpha and beta with heme Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins 1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability Cloning, expression, purification, and preliminary characterization of a putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803. Conformational properties of native sperm whale apomyoglobin in solution Paramagnetic NMR shifts in cyanoferricytochrome c Release of the neocarzinostatin chromophore from the holoprotein does not require major conformational change of the tertiary and secondary structures induced by trifluoroethanol. Novel properties of P450s in Streptomyces coelicolor NMR studies of nitrophorin distal pocket side chain effects on the heme orientation and seating of NP2 as compared to NP1.

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