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Biological functions controlled by manganese redox changes in mononuclear Mn-dependent enzymes
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Outgoing claims: the papers this work cites, builds on, or argues with.
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The structural basis for specificity in lipoxygenase catalysis
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Oxalate decarboxylase: biotechnological update and prevalence of the enzyme in filamentous fungi
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Theoretical study of the catalytic reaction mechanism of MndD
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Characterization of recombinant barley oxalate oxidase expressed by Pichia pastoris
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The redox potential of the system oxygen—superoxide
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Free manganese(II) and iron(II) cations can act as intracellular cell controls
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The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
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The two redox potentials for oxygen reduction to superoxide
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Manganese in Metabolism and Enzyme Function
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The enzymes of oxalate metabolism: unexpected structures and mechanisms
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Molecular enzymology of lipoxygenases
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Characterization of Ceriporiopsis subvermispora bicupin oxalate oxidase expressed in Pichia pastoris
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Expression and characterization of manganese lipoxygenase of the rice blast fungus reveals prominent sequential lipoxygenation of α-linolenic acid
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Metal uptake by manganese superoxide dismutase
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Observation of superoxide production during catalysis of Bacillus subtilis oxalate decarboxylase at pH 4
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Germin, a protein marker of early plant development, is an oxalate oxidase
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Dioxygenase enzymes: catalytic mechanisms and chemical models
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Formation of Hexacoordinate Mn(III) in Bacillus subtilis Oxalate Decarboxylase Requires Catalytic Turnover
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Substrate Binding Mode and Molecular Basis of a Specificity Switch in Oxalate Decarboxylase
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Redox Cycling, pH Dependence, and Ligand Effects of Mn(III) in Oxalate Decarboxylase fromBacillus subtilis
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Steric and Electronic Influence on Proton-Coupled Electron-Transfer Reactivity of a Mononuclear Mn(III)-Hydroxo Complex
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Redox Tuning over Almost 1 V in a Structurally Conserved Active Site: Lessons from Fe-Containing Superoxide Dismutase
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Outer Sphere Mutations Perturb Metal Reactivity in Manganese Superoxide Dismutase,
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Glutamine synthetase from ovine brain is a manganese(II) enzyme
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Potentiometric titrations and oxidation-reduction potentials of several iron superoxide dismutases
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Redox Properties of Human Manganese Superoxide Dismutase and Active-Site Mutants
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Novel Insights into the Basis for Escherichia coli Superoxide Dismutase's Metal Ion Specificity from Mn-Substituted FeSOD and Its Very High Em
inferredcites →https://doi.org/10.1021/bi0200965openalex-snapshot
Structure of Oxalate Decarboxylase from Bacillus subtilis at 1.75 Å Resolution ,
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A Structural Element That Facilitates Proton-Coupled Electron Transfer in Oxalate Decarboxylase
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Oxalate Decarboxylase and Oxalate Oxidase Activities Can Be Interchanged with a Specificity Switch of up to 282 000 by Mutating an Active Site Lid,
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Structural and Kinetic Study of Differences between Human and Escherichia coli Manganese Superoxide Dismutases
inferredcites →https://doi.org/10.1021/bi801856kopenalex-snapshot
Metal Dependence of Oxalate Decarboxylase Activity
inferredcites →https://doi.org/10.1021/bi902106nopenalex-snapshot
An Active Dimanganese(III)−Tyrosyl Radical Cofactor in Escherichia coli Class Ib Ribonucleotide Reductase
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Manganese(II)-Dependent Extradiol-Cleaving Catechol Dioxygenase from Arthrobacter globiformis CM-2
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Crystal Structures of Substrate and Substrate Analog Complexes of Protocatechuate 3,4-Dioxygenase: Endogenous Fe 3+ Ligand Displacement in Response to Substrate Binding ,
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Probing the Active Site of Human Manganese Superoxide Dismutase: The Role of Glutamine 143,
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Probing the Mechanism of Proton Coupled Electron Transfer to Dioxygen: the Oxidative Half-Reaction of Bovine Serum Amine Oxidase
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Superoxide Dismutases and Superoxide Reductases
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Biochemistry and Theory of Proton-Coupled Electron Transfer
inferredcites →https://doi.org/10.1021/cr950053copenalex-snapshot
Manganese Enzymes with Binuclear Active Sites
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Catalytic Reaction Mechanism of Oxalate Oxidase (Germin). A Hybrid DFT Study
inferredcites →https://doi.org/10.1021/ic50018a013openalex-snapshot
Spectra of Manganese(III) Complexes. I. Aquomanganese(III) Ion and Hydroxide, Fluoride, and Chloride Complexes
inferredcites →https://doi.org/10.1021/ic701953gopenalex-snapshot
Modeling the Resting State of Oxalate Oxidase and Oxalate Decarboxylase Enzymes
inferredcites →https://doi.org/10.1021/ic702412yopenalex-snapshot
Spectroscopic and Computational Investigation of Second-Sphere Contributions to Redox Tuning in Escherichia coli Iron Superoxide Dismutase
inferredcites →https://doi.org/10.1021/ja0286977openalex-snapshot
Heavy Atom Isotope Effects on the Reaction Catalyzed by the Oxalate Decarboxylase from Bacillus subtilis
inferredcites →https://doi.org/10.1021/ja2095365openalex-snapshot
Characterization of an O 2 Adduct of an Active Cobalt-Substituted Extradiol-Cleaving Catechol Dioxygenase
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Assigning the EPR Fine Structure Parameters of the Mn(II) Centers in Bacillus subtilis Oxalate Decarboxylase by Site-Directed Mutagenesis and DFT/MM Calculations
inferredcites →https://doi.org/10.1021/ja510666ropenalex-snapshot
Facile Csp2–Csp2 Bond Cleavage in Oxalic Acid-Derived Radicals
inferredcites →https://doi.org/10.1021/ja8052255openalex-snapshot
Electron Paramagnetic Resonance Detection of Intermediates in the Enzymatic Cycle of an Extradiol Dioxygenase
inferredcites →https://doi.org/10.1038/162746a0openalex-snapshot
Order of Stability of Metal Complexes
inferredcites →https://doi.org/10.1038/80954openalex-snapshot
Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.
inferredcites →https://doi.org/10.1038/nature07340openalex-snapshot
Protein-folding location can regulate manganese-binding versus copper- or zinc-binding
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Metalloproteins and metal sensing
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Manganese(ii) chemistry of a new N3O-donor chelate ligand: synthesis, X-ray structures, and magnetic properties of solvent- and oxalate-bound complexes
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Oxygen activation in extradiol catecholate dioxygenases – a density functional study
inferredcites →https://doi.org/10.1042/0264-6021:3430185openalex-snapshot
Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme
inferredcites →https://doi.org/10.1042/bj2530287openalex-snapshot
The potential diagram for oxygen at pH 7
inferredcites →https://doi.org/10.1063/1.555839openalex-snapshot
Standard Electrode Potentials and Temperature Coefficients in Water at 298.15 K
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Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state
inferredcites →https://doi.org/10.1074/jbc.271.30.17687openalex-snapshot
Catalytic Properties of Human Manganese Superoxide Dismutase
inferredcites →https://doi.org/10.1074/jbc.m001408200openalex-snapshot
Kinetics of Manganese Lipoxygenase with a Catalytic Mononuclear Redox Center
inferredcites →https://doi.org/10.1074/jbc.m107202200openalex-snapshot
Oxalate Decarboxylase Requires Manganese and Dioxygen for Activity
inferredcites →https://doi.org/10.1074/jbc.m114.599662openalex-snapshot
Crystal Structure of a Lipoxygenase in Complex with Substrate
inferredcites →https://doi.org/10.1074/jbc.m115.707380openalex-snapshot
Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae
inferredcites →https://doi.org/10.1074/jbc.m313820200openalex-snapshot
A Closed Conformation of Bacillus subtilis Oxalate Decarboxylase OxdC Provides Evidence for the True Identity of the Active Site
inferredcites →https://doi.org/10.1074/jbc.m510256200openalex-snapshot
Structural and Spectroscopic Studies Shed Light on the Mechanism of Oxalate Oxidase
inferredcites →https://doi.org/10.1074/jbc.m609374200openalex-snapshot
Burst Kinetics and Redox Transformations of the Active Site Manganese Ion in Oxalate Oxidase
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Oxalate, Germins, and Higher‐Plant Pathogens
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The Biological Chemistry of the Elements
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Oxalate, germin, and the extracellular matrix of higher plants
inferredcites →https://doi.org/10.1107/s0567739476001551openalex-snapshot
Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides
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Cloning and Sequencing of Two Ceriporiopsis subvermispora Bicupin Oxalate Oxidase Allelic Isoforms: Implications for the Reaction Specificity of Oxalate Oxidases and Decarboxylases
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Bacillus subtilis YvrK Is an Acid-Induced Oxalate Decarboxylase
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Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases
inferredcites →https://doi.org/10.1146/annurev-biochem-070511-100425openalex-snapshot
Photosystem II: The Reaction Center of Oxygenic Photosynthesis
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SUPEROXIDE RADICAL AND SUPEROXIDE DISMUTASES
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The biological chemistry of the elements: the inorganic chemistry of life
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.3390/molecules27031000openalex-snapshot
Dioxygen Reactivity of Copper(I)/Manganese(II)-Porphyrin Assemblies: Mechanistic Studies and Cooperative Activation of O2
inferred← citeshttps://doi.org/10.3390/molecules27061958openalex-snapshot
Comparison of the Content of Several Elements in Seawater, Sea Cucumber Eupentacta fraudatrix and Its High-Molecular-Mass Multiprotein Complex
inferred← citeshttps://doi.org/10.3390/molecules29184414openalex-snapshot
Bidentate Substrate Binding Mode in Oxalate Decarboxylase
inferred← citeshttps://doi.org/10.3390/molecules29194670openalex-snapshot
N-Oxide Coordination to Mn(III) Chloride
inferred← citeshttps://doi.org/10.3390/plants8100381openalex-snapshot
The Biochemical Properties of Manganese in Plants
inferred← citeshttps://doi.org/10.47278/book.vpph/2021.016openalex-snapshot
Preventive Management of the Parasitic Diseases Through Trace Elements
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3openalex-snapshot
Синтез, исследование и моделирование системы хитозан-марганец методами искусственного интеллекта
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.10openalex-snapshot
Модельная реакция синтеза имина из бензиламина
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.11openalex-snapshot
Модельная альдольная реакция
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.12openalex-snapshot
Смоделированный механизм комплексообразования
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.13openalex-snapshot
Термодинамические характеристики комплексообразования
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.14openalex-snapshot
Структура координационных соединений хитозан–металл
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.15openalex-snapshot
Энергетические значения связей
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.16openalex-snapshot
Среднеквадратичное отклонение во времени
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.17openalex-snapshot
Радиальная функция распределения
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.18openalex-snapshot
1H ЯМР смоделированный спектр комплекса хитозан-марганец
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.19openalex-snapshot
Смоделированная дифрактограмма комплекса хитозан-марганец
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.20openalex-snapshot
Смоделированный спектр фотолюминесценции комплекса
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.21openalex-snapshot
Моделирование биологической активности
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.22openalex-snapshot
Сгенерированный программным комплексом снимок СЭМ
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.3openalex-snapshot
Экспериментальные ИК-спектры
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.4openalex-snapshot
Волновые числа максимумов (см-1) полос поглощения комплексов хитозана с Mn2+
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.5openalex-snapshot
Смоделированный ИК-спектр хитозана и комплекса хитозан-марганец
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.6openalex-snapshot
Термические параметры хитозана и комплекса хитозана с Mn2+
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.7openalex-snapshot
Кривые термогравиметрического анализа хитозана и хитозан–Mn2+
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.8openalex-snapshot
Кривые дифференциально-термического анализа хитозана и хитозан–Mn2+
inferred← citeshttps://doi.org/10.60797/chem.2026.9.3.9openalex-snapshot
Дифрактограммы хитозана и комплексов с Mn2+
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