Literature DB >> 11511213

Synthesis and spectroscopic studies of non-heme diiron(III) species with a terminal hydroperoxide ligand: models for hemerythrin.

T J Mizoguchi1, J Kuzelka, B Spingler, J L DuBois, R M Davydov, B Hedman, K O Hodgson, S J Lippard.   

Abstract

Two compounds, [Fe2(mu-OH)(mu-Ph4DBA)(TMEDA)2(OTf)] (4) and [Fe2(mu-OH)(mu-Ph4DBA)(DPE)2(OTf)] (7), where Ph4DBA(2-) is the dinucleating bis(carboxylate) ligand dibenzofuran-4,6-bis(diphenylacetate), have been prepared as synthetic models for the dioxygen-binding non-heme diiron protein hemerythrin (Hr). X-ray crystallography reveals that, in the solid state, these compounds contain the asymmetric coordination environment found at the diiron center in the reduced form of the protein, deoxyHr. Mössbauer spectra of the models (4, delta = 1.21(2), DeltaE(Q) = 2.87(2) mm s(-1); 7, delta(av) = 1.23(1), DeltaE(Qav) = 2.79(1) mm s(-1)) and deoxyHr (delta = 1.19, DeltaE(Q) = 2.81 mm s(-1)) are also in good agreement. Oxygenation of the diiron(II) complexes dissolved in CH2Cl2 containing 3 equiv of N-MeIm (4) or neat EtCN (7) at -78 degrees C affords a red-orange solution with optical bands at 336 nm (7300 M(-1) cm(-1)) and 470 nm (2600 M(-1) cm(-1)) for 4 and at 334 nm (6400 M(-1) cm(-1)) and 484 nm (2350 M(-1) cm(-1)) for 7. These spectra are remarkably similar to that of oxyHr, 330 nm (6800 M(-1) cm(-1)) and 500 nm (2200 M(-1) cm(-1)). The electron paramagnetic resonance (EPR) spectrum of the cryoreduced, mixed-valence dioxygen adduct of 7 displays properties consistent with a (mu-oxo)diiron(II,III) core. An investigation of 7 and its dioxygen-bound adduct by extended X-ray absorption fine structure (EXAFS) spectroscopy indicates that the oxidized species contains a (mu-oxo)diiron(III) core with iron-ligand distances in agreement with those expected for oxide, carboxylate, and amine/hydroperoxide donor atoms. The analogous cobalt complex [Co2(mu-OH)(mu-Ph4DBA)(TMEDA)2(OTf)] (6) was synthesized and structurally characterized, but it was unreactive toward dioxygen.

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Year:  2001        PMID: 11511213     DOI: 10.1021/ic010076b

Source DB:  PubMed          Journal:  Inorg Chem        ISSN: 0020-1669            Impact factor:   5.165


  5 in total

Review 1.  Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.

Authors:  Andrew J Jasniewski; Lawrence Que
Journal:  Chem Rev       Date:  2018-02-05       Impact factor: 60.622

Review 2.  Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites.

Authors:  Loi H Do; Stephen J Lippard
Journal:  J Inorg Biochem       Date:  2011-09-14       Impact factor: 4.155

3.  Noncovalent self-assembly of a heterotetrameric diiron protein.

Authors:  E Neil G Marsh; William F DeGrado
Journal:  Proc Natl Acad Sci U S A       Date:  2002-04-16       Impact factor: 11.205

4.  Active-site structure of a β-hydroxylase in antibiotic biosynthesis.

Authors:  Van V Vu; Thomas M Makris; John D Lipscomb; Lawrence Que
Journal:  J Am Chem Soc       Date:  2011-04-20       Impact factor: 15.419

5.  Magnetic circular dichroism study of a dicobalt(II) complex with mixed 5- and 6-coordination: a spectroscopic model for dicobalt(II) hydrolases.

Authors:  James A Larrabee; W Rainey Johnson; Adam S Volwiler
Journal:  Inorg Chem       Date:  2009-09-21       Impact factor: 5.165

  5 in total

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