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Redox Reactions of Myoglobin

https://doi.org/10.1089/ars.2012.4887

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Proteomics of lipid oxidation‐induced oxidation of porcine and bovine oxymyoglobins

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Structural analysis of fish versus mammalian hemoglobins: Effect of the heme pocket environment on autooxidation and hemin loss

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The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate

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Iron Autoxidation and Free Radical Generation: Effects of Buffers, Ligands, and Chelators

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Enhanced Lipid Oxidation by Oxidatively Modified Myoglobin: Role of Protein-Bound Heme

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Crystal Structures of CO−, Deoxy- and Met-myoglobins at Various pH Values

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Effect of Nitric Oxide on Hemoprotein-Catalyzed Oxidative Reactions

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Myoglobin catalysis in lipid oxidation Assay for activity with linoleic acid as substrate

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Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand

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Equations for the spectrophotometric analysis of hemoglobin mixtures

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Studies on the heterogeneity of hemoglobin

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The multiple effects of ethylenediaminetetraacetate in several model lipid peroxidation systems

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Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin

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Cytochrome c-catalyzed membrane lipid peroxidation by hydrogen peroxide

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Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin

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Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen

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Differential susceptibilities of the prosthetic heme of hemoglobin-based red cell substitutes

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Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts*1

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Sequence of the reaction of heme catabolism catalyzed by the microsomal heme oxygenase system

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The modulation of ferryl myoglobin formation and its oxidative effects on low density lipoproteins by nitric oxide

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Structure and refinement of oxymyoglobin at 1·6 Å resolution

inferredcites →https://doi.org/10.1016/0891-5849(94)90005-1openalex-snapshot

Mechanism of the biphasic effect of ethylenediaminetetraacetate on lipid peroxidation in iron-supported and reconstituted enzymatic system

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Covalent crosslinking of the heme prosthetic group to myoglobin by H2O2: Toxicological implications

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Reduction of hypervalent states of myoglobin and hemoglobin to their ferrous forms by thymoquinone: The role of GSH, NADH and NADPH

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Oxidative stress and vein graft failure: a focus on NADH oxidase, nitric oxide and eicosanoids

inferredcites →https://doi.org/10.1016/j.foodchem.2011.11.060openalex-snapshot

Characteristics of myoglobin and haemoglobin-mediated lipid oxidation in washed mince from bighead carp (Hypophthalmichthys nobilis)

inferredcites →https://doi.org/10.1016/j.foodchem.2012.02.182openalex-snapshot

Retardation of myoglobin and haemoglobin-mediated lipid oxidation in washed bighead carp by phenolic compounds

inferredcites →https://doi.org/10.1016/j.freeradbiomed.2005.09.005openalex-snapshot

Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation

inferredcites →https://doi.org/10.1016/j.semcdb.2012.05.003openalex-snapshot

Redox balance dynamically regulates vascular growth and remodeling

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The lipoxygenase activity of myoglobin. Oxidation of linoleic acid by the ferryl oxygen rather than protein radical.

inferredcites →https://doi.org/10.1016/s0021-9258(17)41764-9openalex-snapshot

His64(E7)–>Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation.

inferredcites →https://doi.org/10.1016/s0021-9258(18)50397-5openalex-snapshot

Metmyoglobin reductase. Identification and purification of a reduced nicotinamide adenine dinucleotide-dependent enzyme from bovine heart which reduces metmyoglobin.

inferredcites →https://doi.org/10.1016/s0021-9258(18)53138-0openalex-snapshot

The mechanism of autooxidation of myoglobin.

inferredcites →https://doi.org/10.1016/s0021-9258(18)55443-0openalex-snapshot

Transmembrane movement of heme.

inferredcites →https://doi.org/10.1016/s0021-9258(18)55444-2openalex-snapshot

The effects of lipid composition on the rate and extent of heme binding to membranes.

inferredcites →https://doi.org/10.1016/s0021-9258(18)62233-1openalex-snapshot

Studies on the Stability of Oxyhemoglobin A and Its Constituent Chains and Their Derivatives

inferredcites →https://doi.org/10.1016/s0021-9258(19)70630-9openalex-snapshot

The stereochemistry of peroxidase catalysis.

inferredcites →https://doi.org/10.1016/s0891-5849(01)00534-2openalex-snapshot

The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species

inferredcites →https://doi.org/10.1016/s0891-5849(99)00240-3openalex-snapshot

Peroxidation of linoleate at physiological pH: hemichrome formation by substrate binding protects against metmyoglobin activation by hydrogen peroxide

inferredcites →https://doi.org/10.1021/bi00027a022openalex-snapshot

Interactions among residues CD3, E7, E10, and E11 in myoglobins: Attempts to simulate the ligand-binding properties of Aplysia myoglobin

inferredcites →https://doi.org/10.1021/bi00152a008openalex-snapshot

High-resolution x-ray structures of pig metmyoglobin and two CD3 mutants: Mb(Lys45 .fwdarw. Arg) and Mb(Lys45 .fwdarw. Ser)

inferredcites →https://doi.org/10.1021/bi011335bopenalex-snapshot

Characteristics and Mechanism of Formation of Peroxide-Induced Heme to Protein Cross-Linking in Myoglobin

inferredcites →https://doi.org/10.1021/bi020647ropenalex-snapshot

Mechanism of Low-Density Lipoprotein Oxidation by Hemoglobin-Derived Iron

inferredcites →https://doi.org/10.1021/bi1001739openalex-snapshot

Straight-Chain Alkyl Isocyanides Open the Distal Histidine Gate in Crystal Structures of Myoglobin,

inferredcites →https://doi.org/10.1021/bi1006942openalex-snapshot

Role of Heme in the Unfolding and Assembly of Myoglobin

inferredcites →https://doi.org/10.1021/bi960372dopenalex-snapshot

Structural Factors Governing Hemin Dissociation from Metmyoglobin

inferredcites →https://doi.org/10.1021/bi960442gopenalex-snapshot

Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin

inferredcites →https://doi.org/10.1021/bi9729413openalex-snapshot

Disruption of the Heme Iron−Proximal Histidine Bond Requires Unfolding of Deoxymyoglobin

inferredcites →https://doi.org/10.1021/bi982729eopenalex-snapshot

Reversible and Irreversible Hemichrome Generation by the Oxygenation of Nitrosylmyoglobin

inferredcites →https://doi.org/10.1021/cr970042eopenalex-snapshot

The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle

inferredcites →https://doi.org/10.1021/ja00051a003openalex-snapshot

Heterolytic versus homolytic peroxide bond cleavage by sperm whale myoglobin and myoglobin mutants

inferredcites →https://doi.org/10.1021/jf00022a004openalex-snapshot

Kinetics and mechanism of thermal oxidation and photooxidation of nitrosylmyoglobin in aqueous solution

inferredcites →https://doi.org/10.1021/jf00037a016openalex-snapshot

Quantitation of heme proteins from spectra of mixtures

inferredcites →https://doi.org/10.1021/jf011535uopenalex-snapshot

Kinetics of Reduction of Ferrylmyoglobin by (−)-Epigallocatechin Gallate and Green Tea Extract

inferredcites →https://doi.org/10.1021/jf0603228openalex-snapshot

Studies with Myoglobin Variants Indicate that Released Hemin Is the Primary Promoter of Lipid Oxidation in Washed Fish Muscle

inferredcites →https://doi.org/10.1021/jf901147aopenalex-snapshot

Phenylalanine Substitution at Site B10 (L29F) Inhibits Metmyoglobin Formation and Myoglobin-Mediated Lipid Oxidation in Washed Fish Muscle: Mechanistic Implications

inferredcites →https://doi.org/10.1021/jf9604798openalex-snapshot

Kinetics and Mechanism of Reduction of Ferrylmyoglobin by Ascorbate and d -Isoascorbate

inferredcites →https://doi.org/10.1021/jf960639fopenalex-snapshot

Prooxidative Activity of Myoglobin Species in Linoleic Acid Emulsions

inferredcites →https://doi.org/10.1021/tx049660yopenalex-snapshot

Desferrioxamine Inhibits Production of Cytotoxic Heme to Protein Cross-Linked Myoglobin: A Mechanism to Protect against Oxidative Stress without Iron Chelation

inferredcites →https://doi.org/10.1023/a:1010268813926openalex-snapshot

Mechanism of Oxidation of Oxymyoglobin by Copper Ions: Comparison of Sperm Whale, Horse, and Pig Myoglobins

inferredcites →https://doi.org/10.1023/a:1023480617038openalex-snapshot

Variability of the Fenton reaction characteristics of the EDTA, DTPA, and citrate complexes of iron

inferredcites →https://doi.org/10.1042/bj0810374openalex-snapshot

The formation and properties of sulphmyoglobin and sulphcatalase

inferredcites →https://doi.org/10.1042/bj20061421openalex-snapshot

Ferryl haem protonation gates peroxidatic reactivity in globins

inferredcites →https://doi.org/10.1042/bss0610065openalex-snapshot

The chemistry of lipid alkoxyl radicals and their role in metal-amplified lipid peroxidation

inferredcites →https://doi.org/10.1073/pnas.0910174107openalex-snapshot

Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure

inferredcites →https://doi.org/10.1074/jbc.272.28.17385openalex-snapshot

Quaternary Structure Regulates Hemin Dissociation from Human Hemoglobin

inferredcites →https://doi.org/10.1074/jbc.274.4.2029openalex-snapshot

Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide

inferredcites →https://doi.org/10.1080/10408398709527457openalex-snapshot

Initiation of lipid peroxidation in biological systems

inferredcites →https://doi.org/10.1080/15216540601178083openalex-snapshot

Histidine and not tyrosine is required for the Peroxide‐induced formation of haem to protein cross‐linked myoglobin

inferredcites →https://doi.org/10.1089/1523086042259823openalex-snapshot

Heme Degradation by Reactive Oxygen Species

inferredcites →https://doi.org/10.1089/ars.2004.6.954openalex-snapshot

The Radical and Redox Chemistry of Myoglobin and Hemoglobin: From In Vitro Studies to Human Pathology

inferredcites →https://doi.org/10.1089/ars.2009.2974openalex-snapshot

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a121739openalex-snapshot

The 2-Electron Reduction of Sperm Whale Ferryl Myoglobin by Ethanol

inferredcites →https://doi.org/10.1111/j.1365-2621.1982.tb12704.xopenalex-snapshot

Measurement and Content of Nonheme and Total Iron in Muscle

inferredcites →https://doi.org/10.1111/j.1745-4514.1992.tb00429.xopenalex-snapshot

SOLUBLE AND BOUND IRON EQUALLY EFFECT LIPID OXIDATION OF SARCOPLASMIC RETICULUM

inferredcites →https://doi.org/10.1159/000020651openalex-snapshot

Pathogenesis of Renal Failure in Rhabdomyolysis: The Role of Myoglobin

inferredcites →https://doi.org/10.1179/135100009x12525712409931openalex-snapshot

Hemin toxicity: a preventable source of brain damage following hemorrhagic stroke

inferredcites →https://doi.org/10.1533/9780857090447.1.77openalex-snapshot

Heme proteins and oxidation in fresh and processed meats

inferredcites →https://doi.org/10.2210/pdb1mgn/pdbopenalex-snapshot

HIS64(E7)-> TYR APOMYOGLOBIN AS A REAGENT FOR MEASURING RATES OF HEMIN DISSOCIATION

inferredcites →https://doi.org/10.3109/10715768709069798openalex-snapshot

Desferrioxamine as an Electron Donor. Inhibition of Membranal Lipid Peroxidation Initiated by H202–Activated Metmyoglobin and Other Peroxidizing Systems

inferredcites →https://doi.org/10.3891/acta.chem.scand.42a-0226openalex-snapshot

Salt Effect on Acid-Catalyzed Autoxidation of Oxymyoglobin.

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Irradiation of myoglobin by intense, ultrashort laser pulses

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Oxidation–reduction imaging of myoglobin reveals two-phase oxidation in the reperfused myocardium

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A novel thermophilic hemoprotein scaffold for rational design of biocatalysts

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Electrochemical determination of heme-linked pKa values and the importance of using fluoride binding in heme proteins

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Epigallocatechin gallate and l-ascorbic acid in conjunction with modified atmospheric packaging preserve color and quality of refrigerated longtail tuna (Thunnus tonggol) slices

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Myoglobin and haemoglobin-mediated lipid oxidation in washed muscle: Observations on crosslinking, ferryl formation, porphyrin degradation, and haemin loss rate

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Changes of sodium nitrate, nitrite, and N-nitrosodiethylamine during in vitro human digestion

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Myoglobin inhibits breast cancer cell fatty acid oxidation and migration via heme-dependent oxidant production and not fatty acid binding

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Synergistic photogeneration of nitric oxide and singlet oxygen by nanofiber membranes via blue and/or red-light irradiation: Strong antibacterial action

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Comparative lipid and heme oxidation of myoglobin, hemoglobin, and cytochrome c in a liposome model

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Ascorbate-catalyzed reductive nitrosylation of ferric myoglobin

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Applications of cold plasma technology for microbiological safety in meat industry

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The effect of dehydrogenase enzyme activity in glycolysis on the colour stability of mutton during postmortem storage

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In Situ Monitoring of Membrane Protein Electron Transfer via Surface-Enhanced Resonance Raman Spectroscopy

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Selective Radical Trifluoromethylation of Native Residues in Proteins

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Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions

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Reactions of persulfides with the heme cofactor of oxidized myoglobin and microperoxidase 11: reduction or coordination

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Development of temperature dependent oxygen releasable nanofilm by modulating oxidation state of myoglobin

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Enhanced treatment uniformity of chemical and biological liquids in cold atmospheric plasma system using gas bubble mixing

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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis -Fe IV state of MauG

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Myoglobin induces mitochondrial fusion, thereby inhibiting breast cancer cell proliferation

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Early prediction of sepsis-induced cardiorenal syndrome: superiority of myoglobin over troponin I

inferred← citeshttps://doi.org/10.1080/1828051x.2023.2240357openalex-snapshot

Role of postmortem bioenergetics in beef colour chemistry

inferred← citeshttps://doi.org/10.1089/ars.2016.6803openalex-snapshot

Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease

inferred← citeshttps://doi.org/10.1101/2023.05.26.542538openalex-snapshot

Oxidation-reduction imaging of myoglobin unveils two-phase oxidation in the reperfused myocardium

inferred← citeshttps://doi.org/10.1111/1541-4337.13040openalex-snapshot

Research progress on quality deterioration mechanism and control technology of frozen muscle foods

inferred← citeshttps://doi.org/10.1111/1750-3841.17378openalex-snapshot

Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model

inferred← citeshttps://doi.org/10.1111/febs.16235openalex-snapshot

Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy

inferred← citeshttps://doi.org/10.1117/12.2510646openalex-snapshot

Genetically encoded FRET probes for direct mapping and quantification of intracellular oxygenation level via fluorescence lifetime imaging

inferred← citeshttps://doi.org/10.1124/pharmrev.121.000564openalex-snapshot

Carbon Monoxide Signaling: Examining Its Engagement with Various Molecular Targets in the Context of Binding Affinity, Concentration, and Biologic Response

inferred← citeshttps://doi.org/10.1152/ajpcell.00167.2019openalex-snapshot

A peroxidase mimetic protects skeletal muscle cells from peroxide challenge and stimulates insulin signaling

inferred← citeshttps://doi.org/10.1152/ajprenal.00394.2016openalex-snapshot

Myoglobin facilitates angiotensin II-induced constriction of renal afferent arterioles

inferred← citeshttps://doi.org/10.1155/2023/5319266openalex-snapshot

Oxidative Stability and Microbial Ecology of Fresh Beef with Extremely Long Shelf-Life

inferred← citeshttps://doi.org/10.1186/s12917-025-04650-xopenalex-snapshot

Sex-dependent metabolic and behavioural alterations in a rat model of forced exertion-induced myopathy

inferred← citeshttps://doi.org/10.1186/s13287-022-02880-6openalex-snapshot

Myoglobin expression by alternative transcript in different mesenchymal stem cells compartments

inferred← citeshttps://doi.org/10.1186/s13287-023-03447-9openalex-snapshot

Bioenergetic profile and redox tone modulate in vitro osteogenesis of human dental pulp stem cells: new perspectives for bone regeneration and repair

inferred← citeshttps://doi.org/10.15586/qas.v15i2.1200openalex-snapshot

Physicochemical and microbiological analysis of goose meat

inferred← citeshttps://doi.org/10.18411/gq-31-03-2018-1openalex-snapshot

General question of world science

inferred← citeshttps://doi.org/10.20996/1819-6446-2021-10-05openalex-snapshot

Endothelial Microvascular Dysfunction and Its Relationship with Haptoglobin Levels in Patients with Different Phenotypes of Chronic Heart Failure

inferred← citeshttps://doi.org/10.21608/jsasj.2022.245702openalex-snapshot

Chemical Preservatives and Microbiological Contamination of Some Locally Processed Meat Products

inferred← citeshttps://doi.org/10.22175/mmb.11689openalex-snapshot

Myoglobin Post-Translational Modifications Influence Color Stability of Beef Longissimus Lumborum

inferred← citeshttps://doi.org/10.22175/mmb2019.07.0025openalex-snapshot

Effects of Oxygen Partial Pressure on 4-Hydroxy-2-Nonenal Induced Oxymyoglobin Oxidation

inferred← citeshttps://doi.org/10.22175/rmc2016.151openalex-snapshot

Effects of Packaging and Temperature on Metmyoglobin Reducing Activity of Cooked Ground Beef Patties

inferred← citeshttps://doi.org/10.31274/etd-180810-4808openalex-snapshot

Electron transfer and redox chemistry in hexa-coordinate hemoglobins

inferred← citeshttps://doi.org/10.3389/fanim.2026.1937601openalex-snapshot

Dietary Ecliptae herba improved growth performance and meat quality possibly associated with gut microbiota and metabolomic changes in Lingshan chickens

inferred← citeshttps://doi.org/10.3390/agriculture13020432openalex-snapshot

Combined Effects of Parsnip Fermented Juice and Hawthorn Extract Regarding Pork Mince Stability: Physico-Chemical and Microbiological Aspects

inferred← citeshttps://doi.org/10.3390/antiox9111109openalex-snapshot

Hemin Prevents Increased Glycolysis in Macrophages upon Activation: Protection by Microbiota-Derived Metabolites of Polyphenols

inferred← citeshttps://doi.org/10.3390/biom16071055openalex-snapshot

Role of Endogenous Myoglobin in Anthracycline Response in Breast Cancer

inferred← citeshttps://doi.org/10.3390/foods15152743openalex-snapshot

Combined Effects of Sodium D-Isoascorbate, Phospholipids and Sodium Lactate on Storage Stability and Shelf Life of Red Sour Soup (Hong Suan Tang) Meat Filling

inferred← citeshttps://doi.org/10.3390/molecules26134033openalex-snapshot

Ginseng Prong Added to Broiler Diets Reduces Lipid Peroxidation in Refrigerated and Frozen Stored Poultry Meats

inferred← citeshttps://doi.org/10.3390/ph15091066openalex-snapshot

Carboxyl Group-Modified Myoglobin Induces TNF-α-Mediated Apoptosis in Leukemia Cells

inferred← citeshttps://doi.org/10.56808/3027-7922.2516openalex-snapshot

Determination of antioxidant property of commercially selling Borneo plants by 2,2′-azino-di-(3-ethylbenzthiazoline- 6-sulfonic acid) free radical scavenging assay

inferred← citeshttps://doi.org/10.6084/m9.figshare.19808915openalex-snapshot

Additional file 1 of Myoglobin expression by alternative transcript in different mesenchymal stem cells compartments

inferred← citeshttps://doi.org/10.70675/3a4dd764ze7d1z4c74zaa58z7527bb36b626openalex-snapshot

Caractérisation de l'influence de facteurs environnementaux sur l'écologie microbienne du jambon cuit tranché.

inferred← citeshttps://doi.org/10.70675/578552b1z332ez4b45za97dz5a97925cb761openalex-snapshot

Détermination des mécanismes impliqués dans la capacité antinitrosante de composés phénoliques. Des extraits végétaux comme solutions pour maîtriser la formation des N-nitrosamines lors de la fabrication et de la digestion de charcuteries

inferred← citeshttps://doi.org/10.70675/7fa2af15z53d9z426cza86az5b5fc10ae3fbopenalex-snapshot

Modification d’acides aminés et de protéines en milieux aqueux sous faisceau d'ions

inferred← citeshttps://doi.org/10.70675/993fac83z1efdz4dd2z8639z1373d18cf659openalex-snapshot

Exposition aux produits de peroxydation lipidique induits par l'apport nutritionnel de fer héminique des viandes : conséquences sur l'homéostasie intestinale et la susceptibilité aux maladies chroniques chez l'adulte et sa descendance

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