Iron porphyrins synthesis

Iron-porphyrins, synthesis and coordination properties of 86PAC1493. Magnetic circular dichroism spectra of -substituted porphyrins 88-ACR95. 

Copper Iron porphyrin synthesis and cytochrome oxidase... 

The synthesis, reactivity, spectroscopy, and electrochemi.stry of organometallic iron porphyrins was de.scribed in some detail in the three reviews published in the period from 1986 to I988. Although a brief synopsis of the early chemistry will be given here, this review will focus on more recent developments. 

Decomposition of diazo compounds by iron porphyrins is a convenient method for the synthesis of non-heteroatom carbene-iron porphyrins [22]. Reaction of [Fe(F2o-TPP)] [F20-TPP = meso-tetrakis(pentafluorophenyl)porphyrinato dianion] with diazo compounds N2C(Ph)R (R = Ph, C02Et, C02CH2CH=CH2) under an inert atmosphere afforded complexes [Fe(F2o-TPP)C(Ph)R] in 65-70% yields (Scheme 2). Like the halocarbene complex [Fe(TPP)(CCl2)], [Fe(F2o-TPP)CPh2] reacted with Melm to afford six-coordinate species [(MeIm)Fe(F2o-TPP)CPh2] in 65% isolated yield. 

Scheme 2 Synthesis of non-heteroatom carbene-iron porphyrins...

Aziridines are versatile intermediates in organic synthesis and commonly found in bioactive molecules. The transition metal-catalyzed nitrene transfer to alkenes is an attractive method for the synthesis of aziridines [7]. In 1984, Mansuy and coworkers reported the first example of an iron-catalyzed alkene aziridination in which iron porphyrin [Fe(TTP)Cl] was used as catalyst and PhINTs was used as nitrene source [30]. Subsequently, the same authors demonstrated that [Fe(TDCPP) (CIO4)] is a more efficient and selective catalyst than [Fe(TTP)Cl] (Scheme 20). 

An anionic ligand effect in iron porphyrin complex-catalyzed competitive epoxidations of cis- and frawi-stilbenes by BU4NHSO5 has been studied in detail . Oxidation of the thiophosphite to the thiophosphate in solid phase oligonucleotide synthesis using BU4NHSO5 was also reported. ... 

Sideroblastic anemia is characterized by excessive iron in the cells that cannot be incorporated into porphyrin to form heme. Although it is rare, the most common cause of sideroblastic anemia is alcoholism and pyridoxine deficiency. Pyridoxine is required for the formation of pyri-doxal phosphate, a coenzyme in porphyrin synthesis. 

Acetylation and formylation are classical reactions in porphyrin chemistry. H. Fischer s synthesis of hemin, for which he was awarded the 1930 Nobel prize, required treatment of deuterohemin (49) with acetic anhydride (or acetyl chloride) in the presence of tin(IV) chloride as a Friedel-Crafts catalyst the product, 3,8-diacetyldeuterohemin-IX (50), was obtained in high yield. Fischer also accomplished formylation of iron porphyrins using dichloromethyl methyl ether and a Friedel-Crafts catalyst (B-37MI30700). Both of Fischer s examples resulted in peripheral substitution of unsubstituted iron porphyrins. However,... 

Scheme 5. Synthesis and reactions of iron-porphyrin vinylidene complexes.

Diederich et al. produced a mimic of the electron-transfer protein cytochrome C. Divergent synthesis afforded a water-soluble iron-porphyrin which possesses a covalently attached dendritic shell surrounding the electrically active heme core which is reminiscent of a protein shell (Fig. 8.7). In contrast to the dendri-... 

The results from the publications mentioned are of interest because they can help in the creation of effective catalytic systems containing porphyrins, which combine functions typical of multienzyme systems. The task in hand is the possible synthesis of bifunctional catalysts based on metalloporphyrin systems, when with the help of manganese porphyrins, for example, or SOD mimic, hydrogen peroxide is accumulated in the system. Afterwards, the accumulated hydrogen peroxide is used in oxidation reactions of various substrates with iron porphyrin components of the catalyst. 

Most patients with Al intoxication develop an erythropoietin-resistant microcytic anemia in the absence of iron deficiency, and this may be a useful early indication of Al toxicity [41,93,254,255]. The chemical similarity between Fe3+ and Al3+ suggest that both elements will have similar metabolic effects, suggesting that iron and Al compete during erythropoiesis, resulting from a reversible block in heme synthesis due either to a defect in porphyrin synthesis or to impaired iron utilization. It was also suggested that the main mechanisms for Al toxicity in the erythropoietic system are the interference of Al in the uptake and utilization of iron and an interaction of Al with cellular membrane components, affecting not only their structures but also their functions [256]. 

In addition to the role of flavoproteins in iron metabolism, it is possible that the anemia associated with riboflavin deficiency is a consequence of the impairment of vitamin Be metabolism in riboflavin deficiency. Pyridoxine oxidase is a flavoprotein and, like glutathione reductase, is very sensitive to riboflavin depletion (McCormick, 1989). Vitamin Be deficiency can result in hypochromic anemia as a result of impaired porphyrin synthesis. Although riboflavin depletion decreases the oxidation of dietary vitamin Be to pyridoxal (Section 9.2), it is not clear to what extent there is secondary vitamin Be deficiency in riboflavin deficiency This is partly because vitamin Be nutritional status is commonly... 

Tryptophan is an essential amino acid involved in synthesis of several important compounds. Nicotinic acid (amide), a vitamin required in the synthesis of NAD+ and NADP+, can be synthesized from tryptophan (Figure 17-24). About 60 mg of tryptophan can give rise to 1 mg of nicotinamide. The synthesis begins with conversion of tryptophan to N-formylkynurenine by tryptophan pyrrolase, an inducible iron-porphyrin enzyme of liver. N-Formylkynurenine is converted to kynurenine by removal of formate, which enters the one-carbon pool. Kynurenine is hydroxylated to 3-hydroxykynurenine, which is converted to 3-hydroxyanthranilate, catalyzed by kynureninase, a pyridoxal phosphate-dependent enzyme. 3-Hydroxyanthranilate is then converted by a series of reactions to nicotinamide ribotide, the immedi-... 

Heme, an iron-porphyrin complex, is the prosthetic group of many important proteins. The central role of hemoglobin and myoglobin in oxygen transport and storage was discussed in Chapter 28. Heme proteins or enzymes are involved in redox reactions (e.g., cytochromes) and participate in many oxidation reactions needed for synthesis of metabolically important compounds as well as for degradation and detoxification of waste products and environmental toxins. 

Biomimetic oxidation catalysis has largely focused on complexes with planar tetradentate ligands such as manganese or iron porphyrins and related macrocyclic trans-chelates[5]. There is considerable interest in the synthesis of multinuclear metal complexes since these molecules might be useful as building block for magnetic molecular materials[6] and model compounds for understanding the properties of metalloproteins[7]. 

N. Nakamura, and Y. Naruta (2001). Synthesis and characterization of alkanethiolate-coordinated iron porphyrins and their dioxygen adducts as models for the active center of cytochrome P450 Direct evidence for hydrogen bonding to bound dioxygen. J. Am. Chem. Soc. 123, 1133-1142. 

Epoxidation. With Mn-salen as a catalyst, enol derivatives give 2-hydroxy acetals. Unsaturated acids form lactones during oxidation in the presence of an iron porphyrin. Glycosylation. The action of a PhlO-MejSiOTf combination on thioglycosides consists of oxidation and Lewis acid catalysis, thus allowing the synthesis of disaccharides. 

An Fe oxidation state, apart from those of catalase and peroxidase compounds 1 and II, is attained only in the carbene complexes, RR C—Fe (Por), nitrene complexes,R N—N=Fe (Por), or the dimeric compounds, Fe (Por)=C=Fe (Por), Fe (Por)=N—Fe or) and [Fe (Por)—O—Fe HPor)]". Both carbene and nitrene complexes are diamagnetic, and the former appear to coordinate RNHj, py, Im, ROH, and RS . They lose the axial ligand in the presence of an excess of pyridine, and form Fe"(Por)(py)2. Though the iron oxidation state in these formally Fe (Por) complexes is still ambiguous, their reactivity implies an iron(III) oxidation state. Attempted synthesis of Fe porphyrins by a one-electron oxidation of Fe (TPP)Cl resulted in formation of the corresponding porphyrin n cation radical Fe "(TPP) . The high oxidation state iron porphyrins are of particular interest in relation to the cytochromes P-450, peroxidases and catalases, and Fe" 0(Por)L (L = 1-MeIm, py, Pip) have been spectroscopically characterized (Scheme 18). - "... 

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