Models for the active site of oxygen-binding hemoproteins. Dioxygen binding properties and the structures of (2-methylimidazole)-meso-tetra(.alpha.,.alpha.,.alpha.,.alpha.-o-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct

Jameson, Geoffrey B.; Molinaro, Frank S.; Ibers, James A.; Coliman, James P.; Brauman, John I.; Rose, Éric; Suslick, Kenneth S.

doi:10.1021/ja00529a055

Cited by 207 publications

(92 citation statements)

References 9 publications

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“…The O 1 -O 2 distance was restrained to be 1.22 Å (e.s.d. 0.01 Å), consistent with that reported by Jameson et al (43). The constraints and restraints used for the bond lengths and bond angles in the porphyrin ring and the imidazole ligand and for the DebyeWaller factors were as described previously (41).…”

Section: Methodssupporting

confidence: 68%

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Dickson

Rich

d’Avigdor

et al. 2013

Journal of Biological Chemistry

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Background: ␣-Hemoglobin stabilizing protein (AHSP) is a hemoglobin chaperone. Results: AHSP causes a subtle perturbation of the proximal heme pocket of O 2 -␣-hemoglobin, lengthening the Fe-O 2 bond and enhancing O 2 dissociation. Conclusion: Pro-30 in wild-type AHSP promotes ␣Hb autooxidation by introducing strain into the proximal heme pocket. Significance: ␣Hb⅐AHSP complexes are intermediates in Hb assembly and achieve ␣Hb detoxification.

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Section: Methodssupporting

confidence: 68%

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Dickson

Rich

d’Avigdor

et al. 2013

Journal of Biological Chemistry

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“…Geometry optimization of [Fe(pfp)(1-MeIm)O 2 ] did not appreciably change the structure from that of the crystal structure 58, 66 and gave first shell bond lengths and angles similar to those found in oxy-heme proteins (SI Table S1). 67,68 …”

Section: Discussionmentioning

confidence: 75%

Iron L-Edge X-ray Absorption Spectroscopy of Oxy-Picket Fence Porphyrin: Experimental Insight into Fe–O₂ Bonding

et al. 2013

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The electronic structure of the Fe–O2 center in oxy-hemoglobin and oxy-myoglobin is a long-standing issue in the field of bioinorganic chemistry. Spectroscopic studies have been complicated by the highly delocalized nature of the porphyrin and calculations require interpretation of multi-determinant wavefunctions for a highly covalent metal site. Here, iron L-edge X-ray absorption spectroscopy (XAS), interpreted using a valence bond configuration interaction (VBCI) multiplet model, is applied to directly probe the electronic structure of the iron in the biomimetic Fe–O2 heme complex [Fe(pfp)(1-MeIm)O2] (pfp = meso-tetra(α,α,α,α-o-pivalamidophenyl) porphyrin or TpivPP). This method allows separate estimates of σ-donor, π-donor, and π-acceptor interactions through ligand to metal charge transfer (LMCT) and metal to ligand charge transfer (MLCT) mixing pathways. The L-edge spectrum of [Fe(pfp)(1-MeIm)O2] is further compared to those of [FeII(pfp)(1-MeIm)2], [FeII(pfp)], and [FeIII(tpp)(ImH)2]Cl (tpp = meso-tetraphenylporphyrin) which have FeII S = 0, FeII S = 1 and FeIII S = 1/2 ground states, respectively. These serve as references for the three possible contributions to the ground state of oxy-pfp. The Fe–O2 pfp site is experimentally determined to have both significant σ-donation and a strong π-interaction of the O2 with the iron, with the latter having implications with respect to the spin polarization of the ground state.

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“…The crystallographic structures of the (noncooperative) solvated solids were obtained 6 and provided some suggestions as to the source of the cooperative interactions.…”

Section: Molecular Solidsmentioning

confidence: 99%

Microporous Porphyrin Solids

et al. 2005

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Metalloporphyrins are exceedingly useful building blocks for the design and synthesis of molecularly based solids. The use of hydrogen bonding or metal ion coordination provides a wide range of framework solids. Using various polyfunctionalized porphyrins, we have created porous solids that are thermally robust and that retain their internal porosity upon loss of solvates. Their pore dimensions are comparable to zeolites, and they show shape and size selectivity in sorption of guest molecules and in epoxidation of alkenes.

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Models for the active site of oxygen-binding hemoproteins. Dioxygen binding properties and the structures of (2-methylimidazole)-meso-tetra(.alpha.,.alpha.,.alpha.,.alpha.-o-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct

Cited by 207 publications

References 9 publications

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Iron L-Edge X-ray Absorption Spectroscopy of Oxy-Picket Fence Porphyrin: Experimental Insight into Fe–O₂ Bonding

Microporous Porphyrin Solids

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Models for the active site of oxygen-binding hemoproteins. Dioxygen binding properties and the structures of (2-methylimidazole)-meso-tetra(.alpha.,.alpha.,.alpha.,.alpha.-o-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct

Cited by 207 publications

References 9 publications

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Iron L-Edge X-ray Absorption Spectroscopy of Oxy-Picket Fence Porphyrin: Experimental Insight into Fe–O2 Bonding

Microporous Porphyrin Solids

Contact Info

Product

Resources

About

Iron L-Edge X-ray Absorption Spectroscopy of Oxy-Picket Fence Porphyrin: Experimental Insight into Fe–O₂ Bonding