Synthetic model compounds for hemoproteins

Traylor, Teddy G.

doi:10.1021/ar00064a002

Cited by 171 publications

(113 citation statements)

References 64 publications

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“…In the absence of added acid, the triprotic iron complex is a logical proton source for the reaction. Consistent with this is the observation that lead(IV) oxide has no effect on the color of solutions of [Fe (4) 2 . In addition, the IR, UV-vis, and ESI-MS spectra of these products were obtained and found to be identical.…”

Section: Synthesis Of Iron(iii) Neutrals Fe(1-3) By Oxidation Of [Fsupporting

confidence: 65%

“…The cationic complexes exhibit a more intense absorption above 1600 cm −1 , whereas the dominant imine absorption in neutral complexes occurs below 1600 cm −1 . It has been previously reported for the 4-imidazolecarboxaldehyde adduct of [FeH 3 (2)](ClO 4 ) 3 that the position of the imine absorption is sensitive to the spin state of iron. 25…”

Section: Characterizationmentioning

confidence: 99%

“…The general stabilization of the iron(II) complexes with the imidazole ligands and the stabilization of the iron(III) forms with the fully deprotonated ligands is pronounced. Although the stabilization of iron(II) with nitrogenous donors is often explained on the basis of the low-spin nature of these complexes, additional factors may be at play in the case of [FeH 3 (2)](ClO 4 ) 2 , which is pure high-spin at room temperature but stable to oxidation in air.…”

Section: Characterizationmentioning

confidence: 99%

“…2 Moreover, deprotonation of the proximal imidazole in several chelated heme model complexes results in immediate oxidization in air, even at low temperatures. 2 Examples of proton-coupled electron transfer (PCET) or the coupling of proton transfer at a coordinated ligand with a metal-centered electron transfer are abundant among transition metal complexes. 3 PCET has been observed among aquo, hydroxo, oxo, 4-7 amine, 8-10 imidazole, 11,12 and other N-heterocyclic 13-15 and oxime 16-18 complexes of transition metal complexes, so it is not surprising that deprotonation of imidazole (or the less extreme case of strong H-bonding) should affect the reduction potential of a metal ion to which it is bound.…”

Section: Introductionmentioning

confidence: 99%

“…The potential for the Fe(III)/Fe(II)couple of [Fe(H 2 (6)) 2 ] 2+ is found at +0.920 mV vs NHE in acetonitrile. Upon deprotonation of the ligands in air (a loss of four protons), spontaneous oxidation is observed, and a new reduction potential is measured at −0.460 mV for Fe (6) 2 − , a negative shift of ~345 mV/proton. The reaction is not reversible on acidification.…”

Section: Introductionmentioning

confidence: 99%

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Proton Control of Oxidation and Spin State in a Series of Iron Tripodal Imidazole Complexes

Brewer¹,

Brewer²,

Luckett³

et al. 2004

Inorg. Chem.

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Section: Synthesis Of Iron(iii) Neutrals Fe(1-3) By Oxidation Of [Fsupporting

confidence: 65%

Section: Characterizationmentioning

confidence: 99%

Section: Characterizationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Proton Control of Oxidation and Spin State in a Series of Iron Tripodal Imidazole Complexes

Brewer¹,

Brewer²,

Luckett³

et al. 2004

Inorg. Chem.

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Miniaturized hemoproteins

et al. 1998

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The present paper highlights and reviews current research in the field of hemoprotein models. Hemoproteins have been extensively studied in order to understand structure‐function relationships, and to design new molecules with desired functions. A wide number of synthetic analogues have been developed, using quite different approaches. They differ in molecular structures, ranging from simple meso‐substituted tetraaryl‐metalloporphyrins and peptide‐porphyrin conjugates. In this paper we summarize the state of the art on peptide based hemoprotein models. We also report here the approach used by us to develop a new class of molecules, named mimochromes. They can be regarded as miniaturized hemoproteins, because mimochromes are low molecular weight compounds with some structural and functional properties common to those of the parent high molecular weight protein. The basic structure of mimochromes is a deuteroporphyrin ring covalently linked to two helical peptide chains. Two molecules of this series have been fully characterized. All the information derived from their structural analysis has been applied to the design of new analogues with additional functions. © 1998 John Wiley & Sons, Inc. Biopoly 47: 5–22, 1998

show abstract

Miniaturized hemoproteins

et al. 1998

View full text Add to dashboard Cite

The present paper highlights and reviews current research in the field of hemoprotein models. Hemoproteins have been extensively studied in order to understand structure-function relationships, and to design new molecules with desired functions. A wide number of synthetic analogues have been developed, using quite different approaches. They differ in molecular structures, ranging from simple meso-substituted tetraaryl-metalloporphyrins and peptide-porphyrin conjugates. In this paper we summarize the state of the art on peptide based hemoprotein models. We also report here the approach used by us to develop a new class of molecules, named mimochromes. They can be regarded as miniaturized hemoproteins, because mimochromes are low molecular weight compounds with some structural and functional properties common to those of the parent high molecular weight protein. The basic structure of mimochromes is a deuteroporphyrin ring covalently linked to two helical peptide chains. Two molecules of this series have been fully characterized. All the information derived from their structural analysis has been applied to the design of new analogues with additional functions.

show abstract

Synthetic model compounds for hemoproteins

Cited by 171 publications

References 64 publications

Proton Control of Oxidation and Spin State in a Series of Iron Tripodal Imidazole Complexes

Proton Control of Oxidation and Spin State in a Series of Iron Tripodal Imidazole Complexes

Miniaturized hemoproteins

Miniaturized hemoproteins

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