Reference health
Effective intermediate-spin iron in O <sub>2</sub> -transporting heme proteins
64/64 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.
4 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 64 checked references that resolve
resolves10.1089/ars.2004.6.954
The Radical and Redox Chemistry of Myoglobin and Hemoglobin: From In Vitro Studies to Human Pathology
resolves10.1073/pnas.1515704112
Discovery of the magnetic behavior of hemoglobin: A beginning of bioinorganic chemistry
resolves10.1016/S0168-6445(03)00056-1
Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology
resolves10.1016/j.jmb.2006.05.036
1.25 Å Resolution Crystal Structures of Human Haemoglobin in the Oxy, Deoxy and Carbonmonoxy Forms
resolves10.1016/S0006-3495(99)77056-6
Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
resolves10.1073/pnas.22.4.210
The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin
resolves10.1007/s00775-011-0763-1
Lessons on O2 and NO bonding to heme from ab initio multireference/multiconfiguration and DFT calculations
resolves10.1016/j.ccr.2012.04.020
Consistent descriptions of metal–ligand bonds and spin-crossover in inorganic chemistry
resolves10.1016/0009-2614(93)89247-F
CASSCF calculation on dioxygen heme complex with extended basis set
resolves10.1021/ja805434m
Nature of the Fe−O<sub>2</sub>Bonding in Oxy-Myoglobin: Effect of the Protein
resolves10.1016/j.jinorgbio.2004.11.008
O2-binding to heme: electronic structure and spectrum of oxyheme, studied by multiconfigurational methods
resolves10.1016/j.bbapap.2013.04.026
How does hemoglobin generate such diverse functionality of physiological relevance?
resolves10.1016/j.pbiomolbio.2005.04.001
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm
resolves10.1016/0968-0004(89)90039-X
Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands
resolves10.1016/j.ccr.2004.04.011
High resolution 1s core hole X-ray spectroscopy in 3d transition metal complexes—electronic and structural information
resolves10.1021/acs.accounts.5b00309
Insights into the Geometric and Electronic Structure of Transition Metal Centers from Valence-to-Core X-ray Emission Spectroscopy
resolves10.1021/ja504182n
Kβ Mainline X-ray Emission Spectroscopy as an Experimental Probe of Metal–Ligand Covalency
resolves10.1021/acs.inorgchem.5b01822
Abrupt versus Gradual Spin-Crossover in Fe<sup>II</sup>(phen)<sub>2</sub>(NCS)<sub>2</sub> and Fe<sup>III</sup>(dedtc)<sub>3</sub> Compared by X-ray Absorption and Emission Spectroscopy and Quantum-Chemical Calculations
resolves10.1039/C3CP53683A
Probing the electronic and geometric structure of ferric and ferrous myoglobins in physiological solutions by Fe K-edge absorption spectroscopy
resolves10.1073/pnas.73.2.491
Structure-function relations in hemoglobin as determined by x-ray absorption spectroscopy.
resolves10.1002/j.1460-2075.1983.tb01605.x
X‐ray absorption near edge structure (XANES) for CO, CN and deoxyhaemoglobin: geometrical information.
resolves10.1002/prot.340100402
Active site conformation in myoglobin as determined by X‐ray absorption spectroscopy
resolves10.1073/pnas.1315734110
X-ray absorption spectroscopic investigation of the electronic structure differences in solution and crystalline oxyhemoglobin
resolves10.1016/j.bbapap.2010.07.019
How different oxidation states of crystalline myoglobin are influenced by X-rays
resolves10.1021/bi00181a019
Spin State and Axial Ligand Bonding in the Hydroxide Complexes of Metmyoglobin, Methemoglobin, and Horseradish Peroxidase at Room and Low Temperatures
resolves10.3389/fphys.2015.00039
Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity
resolves10.1021/acs.biochem.6b00491
Room-Temperature Energy-Sampling Kβ X-ray Emission Spectroscopy of the Mn<sub>4</sub>Ca Complex of Photosynthesis Reveals Three Manganese-Centered Oxidation Steps and Suggests a Coordination Change Prior to O<sub>2</sub> Formation
resolves10.1063/1.1677655
Electronic State of Iron in Hemoglobin, Myoglobin, and Derivatives, as Inferred from X-Ray Fluorescence Spectra
resolves10.1073/pnas.97.2.623
Specific chemical and structural damage to proteins produced by synchrotron radiation
resolves10.1016/j.bbabio.2011.12.010
Structural changes that occur upon photolysis of the Fe(II)a3–CO complex in the cytochrome ba3-oxidase of Thermus thermophilus: A combined X-ray crystallographic and infrared spectral study demonstrates CO binding to CuB
resolves10.1021/bi00269a035
Nuclear magnetic resonance studies of xenon-129 with myoglobin and hemoglobin
resolves10.1007/BF00539228
Magnetic circular dichroism studies of myoglobin, hemoglobin and peroxidase at room and low temperatures. Ferrous high spin derivatives
resolves10.1016/0005-2795(75)90322-0
Studies on the charge transfer band in high spin state of ferric myoglobin and hemoglobin by low temperature optical and magnetic circular dichroism spectroscopy
resolves10.1021/bi00535a004
Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of iron-carbon monoxide stretching and iron-carbon-oxygen bending vibrations and influence of the quaternary structure change
resolves10.1021/bi00281a021
Multiple internal reflectance infrared spectra of variably hydrated hemoglobin and myoglobin films: effects of globin hydration on ligand conformer dynamics and reactivity at the heme
resolves10.1007/s002490050087
Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents
resolves10.1016/0005-2795(79)90137-5
High magnetic field mössbauer studies of deoxymyoglobin, deoxyhemoglobin, and synthetic analogues
resolves10.1002/1521-3773(20010716)40:14<2617::AID-ANIE2617>3.0.CO;2-B
Saddle-Shaped Six-Coordinate Iron(III) Porphyrin Complexes Showing a Novel Spin Crossover betweenS=1/2 andS=3/2 Spin States
resolves10.1021/ja5100367
Resonant Inelastic X-ray Scattering on Ferrous and Ferric Bis-imidazole Porphyrin and Cytochrome <i>c</i>: Nature and Role of the Axial Methionine–Fe Bond
resolves10.1021/ja408072q
Metal–Ligand Covalency of Iron Complexes from High-Resolution Resonant Inelastic X-ray Scattering
resolves10.1021/ja00241a010
Crystal and molecular structure of bis(imidazole)(meso-tetraphenylporphinato)iron(III) chloride. A classic molecule revisited
resolves10.1007/s00425-015-2294-4
Characterization of unusual truncated hemoglobins of Chlamydomonas reinhardtii suggests specialized functions
resolves10.1021/acs.inorgchem.6b01752
Protonation State of MnFe and FeFe Cofactors in a Ligand-Binding Oxidase Revealed by X-ray Absorption, Emission, and Vibrational Spectroscopy and QM/MM Calculations
The 4 references without a DOI — listed, not checked
no DOI — not checkedM Weissbluth Hemoglobin: Cooperativity and Electronic Properties (Springer, Berlin, 1975).
no DOI — not checkedS Pin, B Alpert, A Congiucastellano, SD Longa, A Bianconi, X-ray-absorption spectroscopy of hemoglobin. Hemoglobins. Pt C 232, 266–292 (1994).
no DOI — not checkedLA Piruzian, AA Kuznetsov, VM Chikov, IG Plotnikova, Temperature dependence of the magnetic susceptibility of oxy- and carboxyhemoglobin in the erythrocytes. Izvest Akad Nauk SSSR 6, 894–900 (1984).
no DOI — not checkedMJT Frisch, Gaussian 09, Revision D.01 (Gaussian, Wallingford, CT, 2009).
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.
checked 2026-07-23 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record
Embed this badge
Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.
<a href="https://citestamp.com/citestamped/10.1073/pnas.1706527114"><img src="https://citestamp.com/citestamped/10.1073/pnas.1706527114/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[](https://citestamp.com/citestamped/10.1073/pnas.1706527114)