Complex Formation of Ferric Protoporphyrin IX From the Reaction of Hemin with Ammonia and Small Aliphatic Amines

Reguera, E.; Balmaseda, J.; Fernández‐Bertrán, J.; Paneque, Armando; Yee‐Madeira, H.

doi:10.1023/b:tmch.0000027455.71173.d3

Cited by 2 publications

(2 citation statements)

References 18 publications

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“…Initially, it was expected that H‐E‐NN 1:2 would have the best performance, as it precisely contains the right amount of amine to titrate the carboxylic acids and coordinate to the iron. [ 42 ] However, H‐E‐NN 1:4 exhibited comparable activity in the first cycle. It is likely that in this case the additional free amine available in H‐E‐NN 1:4 plays a similar role to arginine in HRP facilitating the cleavage of the peroxide bond through hydrogen bond formation.…”

Section: Resultsmentioning

confidence: 99%

Hemin‐Doped, Ionically Crosslinked Silicone Elastomers with Peroxidase‐Like Reactivity

Gale

Brook

2021

Adv Funct Materials

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The encapsulation of hemin in polymer systems represents a powerful tool for the preparation of synthetic enzymes. Reported systems largely focus on the creation of hydrogels or microreactors that require a degree of modification to the hemin molecule itself. The straightforward synthesis of hydrophobic hemin‐aminosilicone crosslinked silicone elastomers is described with peroxidase like reactivity. Elastomers are formed from purely ionic interactions between commercial aminoalkylsilicones and native hemin, which acts as a crosslinker. Elastomers prepared from ethylene diamine‐based silicones are robust elastomers in which hemin is retained, while hemin can leach monoamine analogues into the adjacent aqueous environment. The system is easily tunable, allowing for precise control of the hemin concentration and the physical properties of the elastomer. Upon exposure to peroxide‐containing solutions, elastomers readily oxidize the substrate 3′,3′,5′,5′‐tetramethylbenzidine at the interface. Elastomers containing excess amine show greater catalytic efficiency due to the coordination of the amines to the iron center of hemin, which is known to be activating. The reaction can be followed using UV‐visible spectroscopy; rates of reaction and Michaelis–Menten parameters are derived.

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Section: Resultsmentioning

confidence: 99%

Hemin‐Doped, Ionically Crosslinked Silicone Elastomers with Peroxidase‐Like Reactivity

Gale

Brook

2021

Adv Funct Materials

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“…38) It is also well known that histidine, possessing an imidazole moiety, binds to heme, and forms a heme-histidine complex in which two histidine molecules bind to both axial positions of heme, 8,39) suggesting that the mechanism of BH inhibition by histidine is related to its interaction with heme via axial positions. On the other hand, the basic amine group of basic amino acids, has been shown to neutralize the acidic group from two peripheral propionic groups of heme, 40) indicating the capacity of arginine and lysine to complex with heme and to interact and block the active growth site of BH. Furthermore, another amino acid, Lornithine, which is not a natural amino acid but has a structure similar to lysine, was also examined for its effect on BH formation.…”

Section: Inhibition Of Heme Crystallization By Amino Acidsmentioning

confidence: 99%

Effects of Amino Acids on Malarial Heme Crystallization

Uyen

Huy

Trang

et al. 2008

Biological & Pharmaceutical Bulletin

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To gain insight into the mechanism of malarial hemozoin formation and to explore various biological groups for screening novel antimalarial drugs, we examined the effects of amino acids on the formation of b b-hematin (BH), which is a synthetic heme crystal structurally identical to hemozoin, in vitro. Our results showed that BH formation was significantly inhibited by basic amino acids (arginine, lysine, and histidine), probably due to the abilities of these amino acids to complex with heme. The results suggest an involvement in the improvement of the blood-schizonticidal activity of 8-quinolinamine when conjugated with basic amino acids. In addition, cysteine also inhibited BH formation, possibly due to its ability to reduce heme iron or decompose heme in acidic conditions. In contrast, BH formation was enhanced by amino acids with high hydrophobicity values (leucine, isoleucine, valine, methionine, and phenylalanine), with the exception of tryptophan at high temperature but was not affected in Tween-induced BH formation under normal physiological conditions. The present results can lead to further research on the development of new antimalarials by conjugating these amino acids, especially basic amino acids, with other substances, or by forming complex or small peptides that could have special effects on BH formation.

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Complex Formation of Ferric Protoporphyrin IX From the Reaction of Hemin with Ammonia and Small Aliphatic Amines

Cited by 2 publications

References 18 publications

Hemin‐Doped, Ionically Crosslinked Silicone Elastomers with Peroxidase‐Like Reactivity

Hemin‐Doped, Ionically Crosslinked Silicone Elastomers with Peroxidase‐Like Reactivity

Effects of Amino Acids on Malarial Heme Crystallization

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