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Ferryl hemoglobin

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https://www.readbyqxmd.com/read/27642551/differential-heme-release-from-various-hemoglobin-redox-states-and-the-upregulation-of-cellular-heme-oxygenase-1
#1
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
https://www.readbyqxmd.com/read/27527692/effects-of-pharmacological-ascorbate-on-hemoglobin-induced-cancer-cell-proliferation
#2
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
https://www.readbyqxmd.com/read/27470146/engineering-tyrosine-electron-transfer-pathways-decreases-oxidative-toxicity-in-hemoglobin-implications-for-blood-substitute-design
#3
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
https://www.readbyqxmd.com/read/27357070/homolytic-cleavage-of-both-heme-bound-hydrogen-peroxide-and-hydrogen-sulfide-leads-to-the-formation-of-sulfheme
#4
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
https://www.readbyqxmd.com/read/27126166/effects-of-rutin-on-the-redox-reactions-of-hemoglobin
#5
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
https://www.readbyqxmd.com/read/27091316/oxidative-hemoglobin-reactions-applications-to-drug-metabolism
#6
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
https://www.readbyqxmd.com/read/26995402/oxidative-instability-of-hemoglobin-e-%C3%AE-26-glu%C3%A2-lys-is-increased-in-the-presence-of-free-%C3%AE-subunits-and-reversed-by-%C3%AE-hemoglobin-stabilizing-protein-ahsp-relevance-to-hbe-%C3%AE-thalassemia
#7
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
https://www.readbyqxmd.com/read/26987618/self-monitoring-artificial-red-cells-with-sufficient-oxygen-supply-for-enhanced-photodynamic-therapy
#8
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...
2016: Scientific Reports
https://www.readbyqxmd.com/read/26974230/oxidized-ferric-and-ferryl-forms-of-hemoglobin-trigger-mitochondrial-dysfunction-and-injury-in-alveolar-type-i-cells
#9
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
https://www.readbyqxmd.com/read/26782245/the-%C3%AE-lys66tyr-variant-of-human-hemoglobin-as-a-component-of-a-blood-substitute
#10
R S Silkstone, G Silkstone, J A Baath, B Rajagopal, P Nicholls, B J Reeder, L Ronda, L Bulow, C E Cooper
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may be able to reduce the toxicity of the ferryl heme species in extracellular hemoglobin-based oxygen carriers (HBOC) by facilitating long-range electron transfer from endogenous and exogenous antioxidants. Surface-exposed residues lying close to the solvent exposed heme edge may be good candidates for mutations. We therefore studied the properties of the βLys66Tyr mutation. Hydrogen peroxide (H2O2) was added to generate the ferryl protein...
2016: Advances in Experimental Medicine and Biology
https://www.readbyqxmd.com/read/26396189/sickle-cell-hemoglobin-in-the-ferryl-state-promotes-%C3%AE-cys-93-oxidation-and-mitochondrial-dysfunction-in-epithelial-lung-cells-e10
#11
Tigist Kassa, Sirsendu Jana, Michael Brad Strader, Fantao Meng, Yiping Jia, Michael T Wilson, Abdu I Alayash
Polymerization of intraerythrocytic deoxyhemoglobin S (HbS) is the primary molecular event that leads to hemolytic anemia in sickle cell disease (SCD). We reasoned that HbS may contribute to the complex pathophysiology of SCD in part due to its pseudoperoxidase activity. We compared oxidation reactions and the turnover of oxidation intermediates of purified human HbS and HbA. Hydrogen peroxide (H2O2) drives a catalytic cycle that includes the following three distinct steps: 1) initial oxidation of ferrous (oxy) to ferryl Hb; 2) autoreduction of the ferryl intermediate to ferric (metHb); and 3) reaction of metHb with an additional H2O2 molecule to regenerate the ferryl intermediate...
November 13, 2015: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/26391926/interaction-of-the-chlorite-based-drug-wf10-and-chlorite-with-hemoglobin-methemoglobin-and-ferryl-hemoglobin
#12
Annelie Pichert, Jürgen Arnhold
The interaction of the chlorite-based drug solution WF10 with human oxyhemoglobin and oxidized hemoglobin forms was investigated monitoring the corresponding spectral changes in heme states. The chlorite component of WF10 converts oxyhemoglobin into methemoglobin with a rate of 35.4 M(-1)s(-1). Methemoglobin is also formed upon the interaction of ferryl hemoglobin and WF10/chlorite. The rate of this interconversion depends on the oxidation state of ferryl hemoglobin. This rate is 114 M(-1)s(-1), when ferryl hemoglobin was generated upon reaction of oxyhemoglobin and hydrogen peroxide...
November 1, 2015: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/26191198/linoleic-acid-induces-red-blood-cells-and-hemoglobin-damage-via-oxidative-mechanism
#13
Tao Yuan, Wen-Bin Fan, Yu Cong, Hai-Dong Xu, Cheng-Jun Li, Jia Meng, Ni-Rong Bao, Jian-Ning Zhao
Hidden blood loss typically occurs following total hip arthroplasty (THA) and total knee arthroplasty (TKA) and is thought to be related to free fatty acid (FFA). To study the effect of linoleic acid on red blood cells and to examine the pathogenesis of hidden blood loss in vivo, we generated an animal model by injecting linoleic acid into the tail veins of rats. We collected blood samples and determined red blood cell count (RBC) and levels of hemoglobin (Hb), as well as the oxidation and reducing agents in the blood, including glutathione peroxidase (GSH-PX), total superoxide dismutase (T-SOD), hydrogen peroxide (H2O2), and ferryl hemoglobin (Fe4+=O2-), which is generated by the oxidation of Hb...
2015: International Journal of Clinical and Experimental Pathology
https://www.readbyqxmd.com/read/26051522/nitrite-attenuated-hypochlorous-acid-mediated-heme-degradation-in-hemoglobin
#14
Naihao Lu, Jiayu Li, Xiaoming Ren, Rong Tian, Yi-Yuan Peng
Hypochlorous acid (HOCl) is elevated in many inflammatory diseases and causes the accumulation of free iron. Through the Fenton reaction, free iron has the ability to generate free radicals and subsequently is toxic. Recent studies have demonstrated that HOCl participates in heme destruction of hemoglobin (Hb) and free iron release. In this study, it was showed that nitrite (NO2(-)) could prevent HOCl-mediated Hb heme destruction and free iron release. Also, NO2(-) prevented HOCl-mediated loss of Hb peroxidase activity...
August 5, 2015: Chemico-biological Interactions
https://www.readbyqxmd.com/read/25750627/dissection-of-the-radical-reactions-linked-to-fetal-hemoglobin-reveals-enhanced-pseudoperoxidase-activity
#15
Khuanpiroon Ratanasopa, Michael Brad Strader, Abdu I Alayash, Leif Bulow
In the presence of excess hydrogen peroxide (H2O2), ferrous (Fe(+2)) human hemoglobin (Hb) (α2β2) undergoes a rapid conversion to a higher oxidation ferryl state (Fe(+4)) which rapidly autoreduces back to the ferric form (Fe(+3)) as H2O2 is consumed in the reaction. In the presence of additional H2O2 the ferric state can form both ferryl Hb and an associated protein radical in a pseudoperoxidative cycle that results in the loss of radicals and heme degradation. We examined whether adult HbA (β2α2) exhibits a different pseudoenzymatic activity than fetal Hb (γ2α2) due to the switch of γ to β subunits...
2015: Frontiers in Physiology
https://www.readbyqxmd.com/read/25148987/myoglobin-and-haemoglobin-mediated-lipid-oxidation-in-washed-muscle-observations-on-crosslinking-ferryl-formation-porphyrin-degradation-and-haemin-loss-rate
#16
Sung Ki Lee, Nantawat Tatiyaborworntham, Eric W Grunwald, Mark P Richards
Reduced trout haemoglobin (Hb) is a mixture of oxy- and deoxy-Hb at pH 6.3. Addition of oxy/deoxyHb to washed muscle resulted in detectable ferryl Hb while adding bovine oxyHb, trout metHb, or bovine metHb did not. Trout metHb promoted lipid oxidation more rapidly than bovine metHb, attributable to lower haemin affinity in fish Hbs. Protoporphyrin IX degradation was prevalent during trout and bovine Hb-mediated lipid oxidation. Caffeic acid prevented porphyrin degradation and lipid oxidation. Crosslinked myoglobin (Mb) promoted lipid oxidation more effectively than metMb...
January 15, 2015: Food Chemistry
https://www.readbyqxmd.com/read/25046203/electron-paramagnetic-resonance-and-electron-nuclear-double-resonance-studies-of-the-reactions-of-cryogenerated-hydroperoxoferric-hemoprotein-intermediates
#17
Roman Davydov, Mikhail Laryukhin, Amy Ledbetter-Rogers, Masanori Sono, John H Dawson, Brian M Hoffman
The fleeting ferric peroxo and hydroperoxo intermediates of dioxygen activation by hemoproteins can be readily trapped and characterized during cryoradiolytic reduction of ferrous hemoprotein-O2 complexes at 77 K. Previous cryoannealing studies suggested that the relaxation of cryogenerated hydroperoxoferric intermediates of myoglobin (Mb), hemoglobin, and horseradish peroxidase (HRP), either trapped directly at 77 K or generated by cryoannealing of a trapped peroxo-ferric state, proceeds through dissociation of bound H2O2 and formation of the ferric heme without formation of the ferryl porphyrin π-cation radical intermediate, compound I (Cpd I)...
August 5, 2014: Biochemistry
https://www.readbyqxmd.com/read/24972312/evidence-of-the-direct-involvement-of-the-substrate-tcp-radical-in-functional-switching-from-oxyferrous-o2-carrier-to-ferric-peroxidase-in-the-dual-function-hemoglobin-dehaloperoxidase-from-amphitrite-ornata
#18
Shengfang Sun, Masanori Sono, Jing Du, John H Dawson
The coelomic O2-binding hemoglobin dehaloperoxidase (DHP) from the sea worm Amphitrite ornata is a dual-function heme protein that also possesses a peroxidase activity. Two different starting oxidation states are required for reversible O2 binding (ferrous) and peroxidase (ferric) activity, bringing into question how DHP manages the two functions. In our previous study, the copresence of substrate 2,4,6-trichlorophenol (TCP) and H2O2 was found to be essential for the conversion of oxy-DHP to enzymatically active ferric DHP...
August 5, 2014: Biochemistry
https://www.readbyqxmd.com/read/24815022/the-dual-effects-of-nitrite-on-hemoglobin-dependent-redox-reactions
#19
Naihao Lu, Chao Chen, Yingjie He, Rong Tian, Qiang Xiao, Yi-Yuan Peng
Evidence to support the role of heme proteins-dependent reactions as major inducers of oxidative damage is increasingly present. Nitrite (NO2(-)) is one of the major end products of NO metabolism, and from the daily consumption. Although the biological significance of heme proteins/NO2(-)-mediated protein tyrosine nitration is a subject of great interest, the important roles of NO2(-) on heme proteins-dependent redox reactions have been greatly underestimated. In this study, we investigated the influence of NO2(-) on met-hemoglobin (Hb)-dependent oxidative and nitrative stress...
August 31, 2014: Nitric Oxide: Biology and Chemistry
https://www.readbyqxmd.com/read/24698734/tyrosine-can-protect-against-oxidative-stress-through-ferryl-hemoglobin-reduction
#20
Naihao Lu, Yingjie He, Chao Chen, Rong Tian, Qiang Xiao, Yi-Yuan Peng
The toxic mechanism of hemoglobin (Hb) under oxidative stress is linked to the formations of highly cytotoxic ferryl species and subsequently heme-to-protein cross-linked derivative of Hb (Hb-X). In this study, we have examined the effects of free tyrosine and its analogues (3-chlorotyrosine, phenylalanine) on the stability of ferryl hemoglobin and the formation of Hb-X. The results showed that free tyrosine (not phenylalanine, 10-500 μM) was an efficient reducing agent of ferryl species and also effective at preventing the formation of cytotoxic Hb-X...
August 2014: Toxicology in Vitro: An International Journal Published in Association with BIBRA
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