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Ferryl hemoglobin

Denisa Hathazi, Florina Scurtu, Cristina Bischin, Augustin Mot, Amr A A Attia, Jacob Kongsted, Radu Silaghi-Dumitrescu
The autocatalytic reaction between nitrite and the oxy form of globins involves free radicals. For myoglobin (Mb), an initial binding of nitrite to the iron-coordinated oxygen molecule was proposed; the resulting ferrous-peroxynitrate species was not detected, but its decay product, the high-valent ferryl form, was demonstrated in stopped-flow experiments. Reported here are the stopped flow spectra recorded upon mixing oxy Hb (native, as well as chemically-derivatized in the form of several candidates of blood substitutes) with a supraphysiological concentration of nitrite...
February 7, 2018: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
Silvia H Libardi, Fernanda R Alves, Marcel Tabak
The giant extracellular hemoglobin from earthworm Glossoscolex paulistus (HbGp) reacts with hydrogen peroxide, displaying peroxidase activity in the presence of guaiacol. The formation of ferryl-HbGp (compound II) from the peroxidase cycle was studied in the present work. The hypervalent ferryl-HbGp species was formed directly by the reaction of oxy-HbGp and hydrogen peroxide. The oxy-HbGp heme groups (144) under different excess of H2 O2 , relative to heme, showed an influence in the total amount of ferryl-HbGp at the end of the reaction...
May 2018: International Journal of Biological Macromolecules
Nikolette L McCombs, Tatyana Smirnova, Reza A Ghiladi
The use of oxidoreductases as biocatalysts in the syntheses of functionalized, monomeric pyrroles has been a challenge owing to, among a number of factors, undesired polypyrrole formation. Here, we have investigated the ability of dehaloperoxidase (DHP), the coelomic hemoglobin from the terebellid polychaete Amphitrite ornata , to catalyze the H2 O2 -dependent oxidation of pyrroles as a new class of substrate for this enzyme. Substrate oxidation was observed for all compounds employed (pyrrole, N-methylpyrrole, 2-methylpyrrole, 3-methylpyrrole and 2,5-dimethylpyrrole) under both aerobic and anaerobic conditions...
2017: Catalysis Science & Technology
Nantawat Tatiyaborworntham, Mark P Richards
BACKGROUND: Hemoglobin (Hb) is a lipid oxidation promoter in fish muscle. Phospholipase A2 (PLA2; EC is linked to an increased resistance to lipid oxidation of frozen-thawed cod fillets via an unknown mechanism. The present study aimed to investigate the mechanism of Hb-mediated lipid oxidation with a focus on ferryl Hb and methemoglobin (metHb), the pro-oxidative Hb species, and to examine how porcine pancreatic PLA2 inhibits Hb-mediated lipid oxidation in washed cod muscle (WCM)...
November 13, 2017: Journal of the Science of Food and Agriculture
Vladimir V Bamm, Mary E L Henein, Shannon L J Sproul, Danielle K Lanthier, George Harauz
There is a well-documented relationship between cerebral vasculature and multiple sclerosis (MS) lesions: abnormal accumulations of iron have been found in the walls of the dilated veins in cerebral MS plaques. The source of this iron is unknown, but could be related to the recognized phenomenon of capillary and venous hemorrhages leading to blood extravasation. In turn, hemorrhaging leading to hemolysis results in extracellular release of hemoglobin, a reactive molecule that could induce local oxidative stress, inflammation, and tissue damage...
August 31, 2017: Free Radical Biology & Medicine
Haizhou Wu, Jie Yin, Jianhao Zhang, Mark P Richards
Turkey hemolysate promoted lipid oxidation in washed muscle more effectively than pig hemolysate, which was partly attributed to the greater ability of H2O2 that formed during auto-oxidation to oxidize the avian hemoglobin (Hb). Turkey and pig hemolysate (2.5 μM Hb) exposed to 10 μM H2O2 oxidized to 48% and 4% metHb, respectively. Catalase activity, which converts H2O2 to water, was elevated in the pig hemolysate. The larger difference in Hb oxidation when comparing turkey and pig hemolysate in washed muscle (relative to their auto-oxidation rates) suggested that lipid oxidation products facilitated formation of metHb...
September 13, 2017: Journal of Agricultural and Food Chemistry
Tigist Kassa, M B Strader, Akito Nakagawa, Warren M Zapol, Abdu I Alayash
Sickle cell disease (SCD) is an inherited blood disorder caused by a β globin gene mutation of hemoglobin (HbS). The polymerization of deoxyHbS and its subsequent aggregation (into long fibers) is the primary molecular event which leads to red blood cell (RBC) sickling and ultimately hemolytic anemia. We have recently suggested that HbS oxidative toxicity may also contribute to SCD pathophysiology due to its defective pseudoperoxidase activity. As a consequence, a persistently higher oxidized ferryl heme is formed which irreversibly oxidizes "hotspot" residues (particularly βCys93) causing protein unfolding and subsequent heme loss...
September 20, 2017: Metallomics: Integrated Biometal Science
Tao Yuan, Yu Cong, Jia Meng, Hong Qian, Wei Ye, Wen-Shuang Sun, Jian-Ning Zhao, Ni-Rong Bao
BACKGROUND: Hidden blood loss (HBL) often occurs in the prosthetic replacement for joint, but the mechanism is still not clear. MATERIALS AND METHODS: This study tried to establish an animal model of HBL by injecting arachidonic acid (AA) into the Sprague-Dawley rats. Different concentrations of AA were injected into the tail veins of the rats, and blood samples were collected before and after administration at 24, 48, and 72 h. A complete blood count was obtained by to find the hemoglobin (Hb) and red blood cell (RBC) count changes...
May 1, 2017: Journal of Surgical Research
Quan Wang, Ruirui Zhang, Mingzi Lu, Guoxing You, Ying Wang, Gan Chen, Caiyan Zhao, Zhen Wang, Xiang Song, Yan Wu, Lian Zhao, Hong Zhou
Oxidative side reaction is one of the major factors hindering the development of hemoglobin-based oxygen carriers (HBOCs). To avoid the oxidative toxicity, we designed and synthesized polydopamine-coated hemoglobin (Hb-PDA) nanoparticles via simple one-step assemblage without any toxic reagent. Hb-PDA nanoparticles showed oxidative protection of Hb by inhibiting the generation of methemoglobin (MetHb) and ferryl (Fe IV) Hb, as well as excellent antioxidant properties by scavenging free radicals and reactive oxygen species (ROS)...
April 10, 2017: Biomacromolecules
Hong Qian, Tao Yuan, Jian Tong, Wen Shuang Sun, Jiajia Jin, Wen Xiang Chen, Jia Meng, Nirong Bao, Jianning Zhao
OBJECTIVE: Hidden blood loss (HBL), commonly seen after total knee or hip arthroplasty, causes postoperative anemia even after reinfusion or blood transfusion based on the visible blood loss volume. Recent studies demonstrated that oxidative stress might be involved in HBL. However, whether the antioxidants proanthocyanidin (PA) or hydrogen water (HW) can ameliorate HBL remains poorly understood. The aim of this study was to evaluate the effects of PA and HW on HBL. MATERIALS AND METHODS: A rat HBL model was established through administration of linoleic acid with or without treatment with PA or HW...
December 1, 2017: Turkish Journal of Haematology: Official Journal of Turkish Society of Haematology
Fantao Meng, Abdu I Alayash
The role of hemoglobin (Hb) redox forms in tissue and organ toxicities remain ambiguous despite the well-documented contribution of Hb redox reactivity to cellular and subcellular oxidative changes. Moreover, several recent studies, in which Hb toxicity were investigated, have shown conflicting outcomes. Uncertainties over the potential role of these species may in part be due to the protein preparation method of choice, the use of published extinction coefficients and the lack of suitable controls for Hb oxidation and heme loss...
March 15, 2017: Analytical Biochemistry
Tigist Kassa, Sirsendu Jana, Fantao Meng, Abdu I Alayash
Despite advances in our understanding of the oxidative pathways mediated by free hemoglobin (Hb), the precise contribution of its highly reactive redox forms to tissue and organ toxicities remains ambiguous. Heme, a key degradation byproduct of Hb oxidation, has recently been recognized as a damage-associated molecular pattern (DAMP) molecule, able to trigger inflammatory responses. Equally damaging is the interaction of the highly redox active forms of Hb with other biological molecules. We determined the kinetics of heme loss from individual Hb redox states-ferrous (Fe(2+)), ferric (Fe(3+)), and ferryl (Fe(4+))-using two different heme receptor proteins: hemopexin (Hxp), a naturally occurring heme scavenger in plasma, and a double mutant (H64Y/V86F), apomyoglobin (ApoMb), which avidly binds heme released from Hb...
September 2016: FEBS Open Bio
Naihao Lu, Yun Ding, Rong Tian, Zhen Yang, Jianfa Chen, Yi-Yuan Peng
The high heme content in red meat is associated with an increased risk of developing cancer. Pharmacologic concentrations of ascorbate can specifically kill a wide range of cancer cells. In this study, the impact of ascorbate at pharmacologic concentrations on hemoglobin (Hb)-modulated human hepatoma HepG2 cell survival was investigated. It was found that HepG2 cells were proliferated by Hb (5-25μM), but killed by high pharmacologic concentrations of ascorbate (2-10mM). Although ascorbate at the low pharmacologic concentration (0...
November 2016: International Journal of Biological Macromolecules
Gary G A Silkstone, Rebecca S Silkstone, Michael T Wilson, Michelle Simons, Leif Bülow, Kristian Kallberg, Khuanpiroon Ratanasopa, Luca Ronda, Andrea Mozzarelli, Brandon J Reeder, Chris E Cooper
Hemoglobin (Hb)-based oxygen carriers (HBOC) have been engineered to replace or augment the oxygen-carrying capacity of erythrocytes. However, clinical results have generally been disappointing due to adverse side effects linked to intrinsic heme-mediated oxidative toxicity and nitric oxide (NO) scavenging. Redox-active tyrosine residues can facilitate electron transfer between endogenous antioxidants and oxidative ferryl heme species. A suitable residue is present in the α-subunit (Y42) of Hb, but absent from the homologous position in the β-subunit (F41)...
October 1, 2016: Biochemical Journal
Hector D Arbelo-Lopez, Nikolay A Simakov, Jeremy C Smith, Juan Lopez-Garriga, Troy Wymore
Many heme-containing proteins with a histidine in the distal E7 (HisE7) position can form sulfheme in the presence of hydrogen sulfide (H2S) and a reactive oxygen species such as hydrogen peroxide. For reasons unknown, sulfheme derivatives are formed specifically on solvent-excluded heme pyrrole B. Sulfhemes severely decrease the oxygen-binding affinity in hemoglobin (Hb) and myoglobin (Mb). Here, use of hybrid quantum mechanical/molecular mechanical methods has permitted characterization of the entire process of sulfheme formation in the HisE7 mutant of hemoglobin I (HbI) from Lucina pectinata...
August 4, 2016: Journal of Physical Chemistry. B
Naihao Lu, Yun Ding, Zhen Yang, Pingzhang Gao
Flavonoids are widely used to attenuate oxidative damage in vitro and in vivo. In this study, we investigated the influence of rutin (quercetin-3-rhamnosylglucoside) on hemoglobin (Hb)- dependent redox reactions, i.e. oxidative stability of Hb and its cytotoxic ferryl intermediate. It was found that rutin induced generation of H2O2, which in turn oxidized Hb rapidly. Meanwhile, rutin exhibited anti-oxidant effect by effectively reducing ferryl intermediate back to ferric Hb at physiological pH. In comparison with quercetin, rutin had stronger capability on reducing ferryl species while lesser pro-oxidant effect on H2O2 generation, thus it exhibited more protective effect on H2O2-induced Hb oxidation...
August 2016: International Journal of Biological Macromolecules
Tatyana Spolitak, Paul F Hollenberg, David P Ballou
Hb is a protein with multiple functions, acting as an O2 transport protein, and having peroxidase and oxidase activities with xenobiotics that lead to substrate radicals. However, there is a lack of evidence for intermediates involved in these reactions of Hb with redox-active compounds, including those with xenobiotics such as drugs, chemical carcinogens, and sulfides. In particular, questions exist as to what intermediates participate in reactions of either metHb or oxyHb with sulfides. The studies presented here elaborate kinetics and intermediates involved in the reactions of Hb with oxidants (H2O2 and mCPBA), and they demonstrate the formation of high valent intermediates, providing insights into mechanistic issues of sulfur and drug oxidations...
June 15, 2016: Archives of Biochemistry and Biophysics
Michael Brad Strader, Tigist Kassa, Fantao Meng, Francine B Wood, Rhoda Elison Hirsch, Joel M Friedman, Abdu I Alayash
When adding peroxide (H2O2), β subunits of hemoglobin (Hb) bear the burden of oxidative changes due in part to the direct oxidation of its Cys93. The presence of unpaired α subunits within red cells and/or co-inheritance of another β subunit mutant, HbE (β26 Glu→Lys) have been implicated in the pathogenesis and severity of β thalassemia. We have found that although both HbA and HbE autoxidize at initially comparable rates, HbE loses heme at a rate almost 2 fold higher than HbA due to unfolding of the protein...
August 2016: Redox Biology
Zhenyu Luo, Mingbin Zheng, Pengfei Zhao, Ze Chen, Fungming Siu, Ping Gong, Guanhui Gao, Zonghai Sheng, Cuifang Zheng, Yifan Ma, Lintao Cai
Photodynamic therapy has been increasingly applied in clinical cancer treatments. However, native hypoxic tumoural microenvironment and lacking oxygen supply are the major barriers hindering photodynamic reactions. To solve this problem, we have developed biomimetic artificial red cells by loading complexes of oxygen-carrier (hemoglobin) and photosensitizer (indocyanine green) for boosted photodynamic strategy. Such nanosystem provides a coupling structure with stable self-oxygen supply and acting as an ideal fluorescent/photoacoustic imaging probe, dynamically monitoring the nanoparticle biodistribution and the treatment of PDT...
March 18, 2016: Scientific Reports
Narendranath Reddy Chintagari, Sirsendu Jana, Abdu I Alayash
Lung alveoli are lined by alveolar type (AT) 1 cells and cuboidal AT2 cells. The AT1 cells are likely to be exposed to cell-free hemoglobin (Hb) in multiple lung diseases; however, the role of Hb redox (reduction-oxidation) reactions and their precise contributions to AT1 cell injury are not well understood. Using mouse lung epithelial cells (E10) as an AT1 cell model, we demonstrate here that higher Hb oxidation states, ferric Hb (HbFe(3+)) and ferryl Hb (HbFe(4+)) and subsequent heme loss play a central role in the genesis of injury...
August 2016: American Journal of Respiratory Cell and Molecular Biology
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