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The mechanism for the reversible oxygen addition to heme. A theoretical CASPT2 study

https://doi.org/10.1039/b704871h
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29/29 checkable references clean · checked 2026-07-23

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 29 checked references that resolve
resolves10.1021/ar00141a001
Stereochemistry of cooperative mechanisms in hemoglobin
resolves10.1021/cr00027a006
Synthetic Heme-Dioxygen Complexes
resolves10.1021/cr00027a007
Mechanisms of Ligand Recognition in Myoglobin
resolves10.1073/pnas.252590999
Spin-dependent mechanism for diatomic ligand binding to heme
resolves10.1074/jbc.M314007200
How O2 Binds to Heme
resolves10.1002/jcc.20339
On the reversible O<sub>2</sub> binding of the Fe–porphyrin complex
resolves10.1038/203182b0
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
resolves10.1038/202083b0
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
resolves10.1073/pnas.72.6.2335
Ozone Model for Bonding of an O <sub>2</sub> to Heme in Oxyhemoglobin
resolves10.1073/pnas.74.2.398
Magnetic properties of oxyhemoglobin.
resolves10.1073/pnas.81.17.5417
Magnetic susceptibility of oxy- and carbonmonoxyhemoglobins.
resolves10.1016/j.jinorgbio.2004.11.008
O2-binding to heme: electronic structure and spectrum of oxyheme, studied by multiconfigurational methods
resolves10.1016/j.jinorgbio.2005.02.013
Erratum to “O2-binding to heme: electronic structure and spectrum of oxyheme, studied by multiconfigurational methods” [J. Inorg. Biochem. 99(1) (2004) 45–54]
resolves10.1063/1.441662
Electronic structure of iron–dioxygen bond in oxy-Hb-A and its isolated oxy-α and oxy-β chains
resolves10.1021/jp9722115
Equilibrium Geometries and Electronic Structure of Iron−Porphyrin Complexes:  A Density Functional Study
resolves10.1063/1.1682561
Electronic structure of Fe2+ in normal human hemoglobin and its isolated subunits
resolves10.1021/jp0489119
The Spin Dependence of the Spatial Size of Fe(II) and of the Structure of Fe(II)-Porphyrins
resolves10.1063/1.1447902
Electronic structure and bonding in unligated and ligated FeII porphyrins
resolves10.1021/bi00156a030
Oxygen binding constants and stepwise enthalpies for human and bovine hemoglobin at pH 7.6
resolves10.1103/PhysRevB.33.8822
Density-functional approximation for the correlation energy of the inhomogeneous electron gas
resolves10.1103/PhysRevA.38.3098
Density-functional exchange-energy approximation with correct asymptotic behavior
resolves10.1063/1.463096
Fully optimized contracted Gaussian basis sets for atoms Li to Kr
resolves10.1016/S0927-0256(03)00109-5
MOLCAS: a program package for computational chemistry
resolves10.1007/BF01114922
Density matrix averaged atomic natural orbital (ANO) basis sets for correlated molecular wave functions
resolves10.1007/BF01112569
Density matrix averaged atomic natural orbital (ANO) basis sets for correlated molecular wave functions
resolves10.1007/BF01113842
Density matrix averaged atomic natural orbital (ANO) basis sets for correlated molecular wave functions
resolves10.1016/S0006-3495(99)77056-6
Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
resolves10.1016/0009-2614(88)85250-3
MP2 energy evaluation by direct methods
resolves10.1080/00268977000101561
The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors
The 1 reference without a DOI — listed, not checked
no DOI — not checkedb704871h-(cit3)/*[position()=1]
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

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