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description
| - wetenschappelijk artikel (nl)
- article scientifique (publié 2009) (fr)
- наукова стаття, опублікована в травні 2009 (uk)
- im Jahr 2009 veröffentlichter wissenschaftlicher Artikel (de)
- artículu científicu espublizáu en xineru de 2009 (ast)
- artikull shkencor i botuar më 01 janar 2009 (sq)
- scientific article published on 01 January 2009 (en)
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author name string
| - José A Olabe
- Leonardo D Slep
- Valentín T Amorebieta
- Andrea C Montenegro
- Diego F Martín
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rdfs:label
| - Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (en)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (nl)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (sq)
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skos:prefLabel
| - Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (en)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (nl)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (sq)
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name
| - Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (en)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (nl)
- Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform (sq)
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title
| - Three redox states of nitrosyl: NO+, NO*, and NO-/HNO interconvert reversibly on the same pentacyanoferrate(II) platform (en)
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is owl:sameAs
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is cites work
of | - Insights into the nitric oxide reductase mechanism of flavodiiron proteins from a flavin-free enzyme
- Reactions of HNO with heme proteins: new routes to HNO-heme complexes and insight into physiological effects.
- HNO binding in a heme protein: structures, spectroscopic properties, and stabilities.
- Computational investigations of HNO in biology.
- Acidity and hydrogen exchange dynamics of iron(II)-bound nitroxyl in aqueous solution
- A thermally stable {FeNO}8complex: properties and biological reactivity of reduced MNO systems
- Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide.
- Nitroxyl as a ligand in ruthenium tetraammine systems: a density functional theory study
- Metal centre effects on HNO binding in porphyrins and the electronic origin: metal's electronic configuration, position in the periodic table, and oxidation state
- Mechanism elucidation of the cis-trans isomerization of an azole ruthenium-nitrosyl complex and its osmium counterpart
- Isolation of a radical dianion of nitrogen oxide (NO)(2-).
- Nitric oxide insertion reactivity with the bismuth-carbon bond: formation of the oximate anion, [ON=(C6H2tBu2O)]-, from the oxyaryl dianion, (C6H2tBu2O)2-.
- A Nonheme, High-Spin {FeNO}8 Complex that Spontaneously Generates N2O.
- Nitric oxide activation facilitated by cooperative multimetallic electron transfer within an iron-functionalized polyoxovanadate–alkoxide cluster
- A Nonheme Sulfur-Ligated {FeNO} Complex and Comparison with Redox-Interconvertible {FeNO} and {FeNO} Analogues
- A Mononuclear, Nonheme FeII-Piloty's Acid (PhSO2NHOH) Adduct: An Intermediate in the Production of {FeNO}7/8 Complexes from Piloty's Acid.
- Tracing the Iron Nitrosyl Complex [Fe(2,2′-bipyridine)(CN)3(NO)]-
- Nitrosyl- versus nitroxyl-cobalamin?
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