Reaction between Lipid Hydroperoxide and Hemoglobin Studied by a Spectrophotometric and a Spin Trapping Method

Aoshima, Hitoshi; Yoshida, Yasushi; Taniguchi, Hiroki

doi:10.1080/00021369.1986.10867648

Cited by 3 publications

(2 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The destiny of this alkoxyl radical is usually either to rearrange to form an epoxyl alkyl radical which then react with oxygen to form LOO•, or to react with another lipid radical to generate an alcohol and a further lipid alkyl radical [14][15][16]. Lipid hydroperoxides can also react with the ferryl group to reform ferric heme and generate a further peroxyl radical: P-Fe 4+ -OH -+ LOOH → P-Fe 3+ + LOO• + OHThus Mb and Hb can function as both pro-oxidant and pseudo-peroxidase enzymes to both initiate and feed a cascade cycle of lipid oxidation [17][18][19] (Scheme 1).…”

Section: The Redox and Radical Chemistry Of Myoglobin And Hemoglobinmentioning

confidence: 99%

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

Reeder¹,

Wilson

2005

CMC

149

111

View full text Add to dashboard Cite

The heme based respiratory proteins myoglobin and hemoglobin can, under certain conditions, exhibit a peroxidase-like enzymic activity, in which a catalytic cycle, driven by peroxides, leads to oxidation of bio molecules. These heme proteins are implicated in what is termed "oxidative stress" as this catalytic cycle, when it occurs in vivo, generates cytotoxic product that are implicated in the pathology of a number of disease states. Here we review the evidence that such reactions occur in vivo, in particular in animal models and human patients and examine the underlying chemical mechanism. This mechanism involves the production of ferryl heme (Fe(IV)=O(2-)) and it is this and associated radicals that initiate processes such as lipid peroxidation and the generation of bioactive molecules such as isoprostanes. The reactivity of the high oxidation state of the heme also allows us to identify unambiguous biomarkers for its presence in vivo in such conditions as rhabdomyolysis and brain hemorrhage. Ways to inhibit the peroxidatic cycle are discussed and the role of iron chelators such as desferrioxamine is discussed in terms of their often neglected properties as reducing agents. Suppression of the peroxidatic activity of hemoglobin is discussed in the context of the development of blood substitutes.

show abstract

Section: The Redox and Radical Chemistry Of Myoglobin And Hemoglobinmentioning

confidence: 99%

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

Reeder¹,

Wilson

2005

CMC

149

111

View full text Add to dashboard Cite

show abstract

“…These circular reaction systems produced both alkoxyl (RO • ) and peroxyl (ROO • ) radicals. 49 Step 1: hemin reacts with H 2 O 2 to form ferryl hemin along with various radical species capable of oxidizing substrates such as the heme moiety or the protein.…”

Section: H 2 O 2 Determinationmentioning

confidence: 99%

A biomimetic enzyme modified electrode for H₂O₂ highly sensitive detection

Kong

et al. 2015

Analyst

View full text Add to dashboard Cite

An efficient catalyst based on artificial bionic peroxidase was synthesized for electrocatalysis. A poly(ethyleneimine)/Au nanoparticle composite (PEI-AuNP) was prepared and it was then linked to hemin via a coupling reaction between carboxyl groups in hemin and amino groups in PEI without the activation of a carboxyl group by carbodiimide. Fourier transform infrared (FTIR) spectroscopy verified the formation of amido bonds within the structure. The presence of AuNPs contributed greatly in establishing the amido bonds within the composite. Transmission electron microscopy (TEM) and UV-visible spectroscopy were also used to characterize the PEI-AuNP-hemin catalyst. PEI-AuNP-hemin exhibited intrinsic peroxidase-like catalytic activities. The PEI-AuNP-hemin deposited on a glass carbon electrode had strong sensing for H2O2 with a well-defined linear relationship between the amperometric response and H2O2 concentration in the range from 1 μM to 0.25 mM. The detection limit was 0.247 nM with a high sensitivity of 0.347 mA mM(-1) cm(-2). The peroxidase-like catalytic activity of PEI-AuNP-hemin is discussed in relation to its microstructure. The study suggests that PEI-AuNP-hemin may have promising application prospects in biocatalysis and bioelectronics.

show abstract

Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control

Vlasova

2018

Molecules

110

View full text Add to dashboard Cite

The heme in the active center of peroxidases reacts with hydrogen peroxide to form highly reactive intermediates, which then oxidize simple substances called peroxidase substrates. Human peroxidases can be divided into two groups: (1) True peroxidases are enzymes whose main function is to generate free radicals in the peroxidase cycle and (pseudo)hypohalous acids in the halogenation cycle. The major true peroxidases are myeloperoxidase, eosinophil peroxidase and lactoperoxidase. (2) Pseudo-peroxidases perform various important functions in the body, but under the influence of external conditions they can display peroxidase-like activity. As oxidative intermediates, these peroxidases produce not only active heme compounds, but also protein-based tyrosyl radicals. Hemoglobin, myoglobin, cytochrome c/cardiolipin complexes and cytoglobin are considered as pseudo-peroxidases. Рeroxidases play an important role in innate immunity and in a number of physiologically important processes like apoptosis and cell signaling. Unfavorable excessive peroxidase activity is implicated in oxidative damage of cells and tissues, thereby initiating the variety of human diseases. Hence, regulation of peroxidase activity is of considerable importance. Since peroxidases differ in structure, properties and location, the mechanisms controlling peroxidase activity and the biological effects of peroxidase products are specific for each hemoprotein. This review summarizes the knowledge about the properties, activities, regulations and biological effects of true and pseudo-peroxidases in order to better understand the mechanisms underlying beneficial and adverse effects of this class of enzymes.

show abstract

Reaction between Lipid Hydroperoxide and Hemoglobin Studied by a Spectrophotometric and a Spin Trapping Method

Cited by 3 publications

References 7 publications

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

A biomimetic enzyme modified electrode for H₂O₂ highly sensitive detection

Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control

Contact Info

Product

Resources

About

Reaction between Lipid Hydroperoxide and Hemoglobin Studied by a Spectrophotometric and a Spin Trapping Method

Cited by 3 publications

References 7 publications

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States

A biomimetic enzyme modified electrode for H2O2 highly sensitive detection

Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control

Contact Info

Product

Resources

About

A biomimetic enzyme modified electrode for H₂O₂ highly sensitive detection