Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
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Bovine cytochrome c oxidase structures enable O 2 reduction with minimization of reactive oxygens and provide a proton-pumping gateSite-selective Characterization of Src Homology 3 Domain Molecular Recognition with Cyanophenylalanine Infrared Probes.Time-resolved visible and infrared study of the cyano complexes of myoglobin and of hemoglobin I from Lucina pectinata.Elucidating Oxygen Reduction Active Sites in Pyrolyzed Metal-Nitrogen Coordinated Non-Precious-Metal Electrocatalyst SystemsCyanide: a strong-field ligand for ferrohemes and hemoproteins?Comparison of cyanide and carbon monoxide as ligands in iron(II) porphyrinatesRedox interactions in cytochrome c oxidase: from the "neoclassical" toward "modern" models.Investigations of ferric heme cyanide photodissociation in myoglobin and horseradish peroxidase.Vibrational stark effect probes for nucleic acidsBis(cyano) Iron(III) Porphyrinates: What Is the Ground State?Investigations of vibrational coherence in the low-frequency region of ferric heme proteins.Geometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: vibrational and ENDOR studiesNew insights on the electronic and molecular structure of cyanide-ligated iron(III) porphyrinatesMechanism of interaction between the general anesthetic halothane and a model ion channel protein, III: Molecular dynamics simulation incorporating a cyanophenylalanine spectroscopic probe.Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, II: Fluorescence and vibrational spectroscopy using a cyanophenylalanine probeAcyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase-Carrier Protein Cross-Link.Selective incorporation of nitrile-based infrared probes into proteins via cysteine alkylationPhotochemical and ligand-exchange properties of the cyanide complex of fully reduced cytochrome c oxidase.Redox- and anion-linked protonation sites in horseradish peroxidase: analysis of distal haem pocket mutants.When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase
P2860
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P2860
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
description
1985 nî lūn-bûn
@nan
1985 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի մարտին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
name
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@ast
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@en
type
label
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@ast
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@en
prefLabel
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@ast
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@en
P2093
P1476
Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.
@en
P2093
D H O'Keeffe
S Yoshikawa
W S Caughey
P304
P407
P577
1985-03-01T00:00:00Z