How O2 binds to heme: reasons for rapid binding and spin inversion.
about
Structure of the processive rubber oxygenase RoxA from Xanthomonas spFe L-edge X-ray absorption spectroscopy of low-spin heme relative to non-heme Fe complexes: delocalization of Fe d-electrons into the porphyrin ligand.Positively selected sites in cetacean myoglobins contribute to protein stability.Structural basis for cooperative binding of azoles to CYP2E1 as interpreted through guided molecular dynamics simulations.Local changes in arterial oxygen saturation induced by visible and near-infrared light radiation.Effects of imidazole deprotonation on vibrational spectra of high-spin iron(II) porphyrinates.Iron L-edge X-ray absorption spectroscopy of oxy-picket fence porphyrin: experimental insight into Fe-O2 bonding.Water may inhibit oxygen binding in hemoprotein models.Binding of O2 and NO to heme in heme-nitric oxide/oxygen-binding (H-NOX) proteins. A theoretical study.Ambidentate H-bonding of NO and O2 in heme proteinsCO, NO and O2 as Vibrational Probes of Heme Protein Interactions.Catalytic oxygen activation versus autoxidation for industrial applications: a physicochemical approach.Heme isomers substantially affect heme's electronic structure and function.Lessons on O2 and NO bonding to heme from ab initio multireference/multiconfiguration and DFT calculations.Just a proton: distinguishing the two electronic states of five-coordinate high-spin iron(II) porphyrinates with imidazole/ate coordination.Electronic structure and ligand vibrations in FeNO, CoNO, and FeOO porphyrin adducts.Intermediate P* from soluble methane monooxygenase contains a diferrous cluster.Accurate ab initio potential energy curve of O2. II. Core-valence correlations, relativistic contributions, and vibration-rotation spectrum.O2 binding to heme is strongly facilitated by near-degeneracy of electronic states.Biomimetic iron(III) complexes of facially and meridionally coordinating tridentate 3N ligands: tuning of regioselective extradiol dioxygenase activity in organized assemblies.An electrospray ionization mass spectrometry study of azidoacetic acid/transition metal complexes.Towards quantifying the role of exact exchange in predictions of transition metal complex properties.Water as biocatalyst in cytochrome P450
P2860
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P2860
How O2 binds to heme: reasons for rapid binding and spin inversion.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
How O2 binds to heme: reasons for rapid binding and spin inversion.
@en
How O2 binds to heme: reasons for rapid binding and spin inversion.
@nl
type
label
How O2 binds to heme: reasons for rapid binding and spin inversion.
@en
How O2 binds to heme: reasons for rapid binding and spin inversion.
@nl
prefLabel
How O2 binds to heme: reasons for rapid binding and spin inversion.
@en
How O2 binds to heme: reasons for rapid binding and spin inversion.
@nl
P2860
P356
P1476
How O2 binds to heme: reasons for rapid binding and spin inversion.
@en
P2093
Kasper P Jensen
P2860
P304
14561-14569
P356
10.1074/JBC.M314007200
P407
P577
2004-01-29T00:00:00Z