The iron–oxygen bond in human oxyhaemoglobin

The iron–oxygen bond in human oxyhaemoglobin

Item
http://www.wikidata.org/entity/Q59068067
An investigation by iron K-edge spectroscopy of the oxidation state of iron in hemoglobin and its subunits.New perspectives on iron-ligand vibrations of oxyheme complexes.Lessons on O2 and NO bonding to heme from ab initio multireference/multiconfiguration and DFT calculations.The alpha 1 beta 1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen.Biomimic O2 activation hydroxylates a meso-carbon of the porphyrin ring regioselectively under mild conditions.Mössbauer spectroscopy of haemoglobins. Study of the relationship of Fe2+ electronic and molecular structure of the active site.H2O2 determination by a biosensor based on hemoglobin.Employing aqueous CdTe quantum dots with diversified surface functionalities to discriminate between heme (Fe(ii)) and hemin (Fe(iii))Accessing nature's inorganic secrets
P2860

The iron–oxygen bond in human oxyhaemoglobin

Item
http://www.wikidata.org/entity/Q59068067
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature у квітні 1982
@uk
name
The iron–oxygen bond in human oxyhaemoglobin
@en
The iron–oxygen bond in human oxyhaemoglobin
@nl
type
label
The iron–oxygen bond in human oxyhaemoglobin
@en
The iron–oxygen bond in human oxyhaemoglobin
@nl
prefLabel
The iron–oxygen bond in human oxyhaemoglobin
@en
The iron–oxygen bond in human oxyhaemoglobin
@nl
P1433
P1476
P2093
P2888
P304
P31
P356
P407
P433
P478
P50
P577
P6179
P698
P356
P1433
P1476
The iron-oxygen bond in human oxyhaemoglobin
@en
P2093
P2888
P304
P31
P356
P407
P433
P478
P50
P577
P6179
P698