Direct Magnetic Resonance Evidence for Peroxymonocarbonate Involvement in the Cu,Zn-Superoxide Dismutase Peroxidase Catalytic Cycle

Gabel, Scott A.; Ranguelova, Kalina; Stadler, Krisztián; DeRose, Eugene F.; London, Robert E.; Mason, Ronald P.

doi:10.1074/jbc.m804644200

Cited by 24 publications

(31 citation statements)

References 51 publications

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“…То есть конечные продукты реакции автоокисления адреналина, кроме адренохрома, могут быть не только супероксид анионы, но и радикалы карбонат/бикарбонатного буфера и диоксида углерода, растворённого в буфере. Такое наше предположение основывается на данных современной литературы, где активно обсуждается существование и роль карбонатных радикалов и радикалов диоксида углерода [30][31][32][33][34][35][36][37][38]42].…”

Section: рисунокunclassified

“…Изучая молекулярный механизм пероксидазного действия Cu-Zn-СОД, было показано, что важным и необходимым участником реакции является бикарбонатный ион (НСО 3 -), который, взаимодействуя с пероксидом водорода, образует промежуточный интермедиат пероксимонокарбонат (НООСО 2 -), формирующий затем карбонат анион радикал (СО 3 -· ) [30][31][32][33][34][35]. В условиях исследуемой нами реакции автоокисления адреналина присутствуют следующие компоненты: буфер Na 2 CO 3 -NaHCO 3 , растворённые в буфере атмосферные О 2 и СО 2 и вносится адреналин; в процессе его окисления высвобождаются электроны.…”

Section: рисунокunclassified

“…Таким образом, в реакционной среде, где происходит автоокисление адреналина, кроме названных выше соединений, есть и образовавшийся пероксид водорода. Спонтанное взаимодействие пероксида водорода и бикарбонатных ионов, как описано в работах [30][31][32][33][34][35], может приводить к образованию промежуточного продукта пероксимонокарбоната, из которого и возникает затем карбонатный анион радикал. Экспериментальные доказательства такого хода событий представлены в работе [34].…”

Section: рисунокunclassified

“…Спонтанное взаимодействие пероксида водорода и бикарбонатных ионов, как описано в работах [30][31][32][33][34][35], может приводить к образованию промежуточного продукта пероксимонокарбоната, из которого и возникает затем карбонатный анион радикал. Экспериментальные доказательства такого хода событий представлены в работе [34]. В этом направлении также ведутся исследования, описанные в работах [30][31][32][33]35].…”

Section: рисунокunclassified

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Involvement of carbonate/bicarbonate ions in the superoxide-generating reaction of adrenaline autoxidation

Sirota

2015

BIOMED KHIM

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An important role of carbonate/bicarbonate ions has been recognized in the superoxide generating reaction of adrenaline autooxidation in an alkaline buffer (a model of quinoid adrenaline oxidation in the body). It is suggested that these ions are directly involved not only in formation of superoxide anion radical (О2 -·) but also other radicals derived from the carbonate/bicarbonate buffer. Using various buffers it was shown that the rate of accumulation of adrenochrome, the end product of adrenaline oxidation, and the rate of О2 -· formation depend on concentration of carbonate/bicarbonate ions in the buffer and that these ions significantly accelerate adrenaline autooxidation thus demonstrating prooxidant properties. The detectable amount of diformazan, the product of nitro blue tetrazolium (NBT) reduction, was significantly higher than the amount of adrenochrome formed; taking into consideration the literature data on О2 -· detection by NBT it is suggested that adrenaline autooxidation is accompanied by one-electron reduction not only of oxygen dissolved in the buffer and responsible for superoxide formation but possible carbon dioxide also dissolved in the buffer as well as carbonate/bicarbonate buffer components leading to formation of corresponding radicals. The plots of the dependence of the inhibition of adrenochrome and diformazan formation on the superoxide dismutase concentration have shown that not only superoxide radicals are formed during adrenaline autooxidation. Since carbonate/bicarbonate ions are known to be universally present in the living nature, their involvement in free radical processes proceeding in the organism is discussed.

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Section: рисунокunclassified

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Involvement of carbonate/bicarbonate ions in the superoxide-generating reaction of adrenaline autoxidation

Sirota

2015

BIOMED KHIM

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“…In some cases, peroxidase activity can generate superoxide from H 2 O 2 , and a hydroxyl radical that modifies the imidazole ring of histidine, which irreversibly inactivates the enzyme (33,34). If cellular conditions favor it, H 2 O 2 can react with carbonate to form peroxymonocarbonate, which can also be processed by the enzyme to create the carbonate radical (4,37,70).…”

Section: Figmentioning

confidence: 99%

Regulation of CuZnSOD and Its Redox Signaling Potential: Implications for Amyotrophic Lateral Sclerosis

Hitchler

Domann

2014

Antioxidants & Redox Signaling

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Significance: Molecular oxygen is a Janus-faced electron acceptor for biological systems, serving as a reductant for respiration, or as the genesis for oxygen-derived free radicals that damage macromolecules. Superoxide is well known to perturb nonheme iron proteins, including Fe/S proteins such as aconitase and succinate dehydrogenase, as well as other enzymes containing labile iron such as the prolyl hydroxylase domain-containing family of enzymes; whereas hydrogen peroxide is more specific for two-electron reactions with thiols on glutathione, glutaredoxin, thioredoxin, and the peroxiredoxins. Recent Advances: Over the past two decades, familial cases of amyotrophic lateral sclerosis (ALS) have been shown to have an association with commonly altered superoxide dismutase 1 (SOD1) activity, expression, and protein structure. This has led to speculation that an altered redox balance may have a role in creating the ALS phenotype. Critical Issues: While SOD1 alterations in familial ALS are manifold, they generally create perturbations in the flux of electrons. The nexus of SOD1 between one-and two-electron signaling processes places it at a key signaling regulatory checkpoint for governing cellular responses to physiological and environmental cues. Future Directions: The manner in which ALS-associated mutations adjust SOD1's role in controlling the flow of electrons between one-and two-electron signaling processes remains obscure. Here, we discuss the ways in which SOD1 mutations influence the form and function of copper zinc SOD, the consequences of these alterations on free radical biology, and how these alterations might influence cell signaling during the onset of ALS. Antioxid. Redox Signal. 20, 1590Signal. 20, -1598

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Redox control of enzymatic functions: The electronics of life's circuitry

et al. 2014

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The field of redox biology has changed tremendously over the past 20 years. Formerly regarded as bi-products of the aerobic metabolism exclusively involved in tissue damage, reactive oxygen species (ROS) are now recognized as active participants of cell signaling events in health and in disease. In this sense, ROS and the more recently defined reactive nitrogen species (RNS) are, just like hormones and second messengers, acting as fundamental orchestrators of cell signaling pathways. The chemical modification of enzymes by ROS and RNS (that result in functional enzymatic alterations) accounts for a considerable fraction of the transient and persistent perturbations imposed by variations in oxidant levels. Upregulation of ROS and RNS in response to stress is a common cellular response that foments adaptation to a variety of physiologic alterations (hypoxia, hyperoxia, starvation, and cytokine production). Frequently, these are beneficial and increase the organisms' resistance against subsequent acute stress (preconditioning). Differently, the sustained ROS/RNSdependent rerouting of signaling produces irreversible alterations in cellular functioning, often leading to pathogenic events. Thus, the duration and reversibility of protein oxidations define whether complex organisms remain "electronically" healthy. Among the 20 essential amino acids, four are particularly susceptible to oxidation: cysteine, methionine, tyrosine, and tryptophan. Here, we will critically review the mechanisms, implications, and repair systems involved in the redox modifications of these residues in proteins while analyzing well-characterized prototypic examples. Occasionally, we will discuss potential consequences of amino acid oxidation and speculate on the biologic necessity for such events in the context of adaptative redox signaling.

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Direct Magnetic Resonance Evidence for Peroxymonocarbonate Involvement in the Cu,Zn-Superoxide Dismutase Peroxidase Catalytic Cycle

Cited by 24 publications

References 51 publications

Involvement of carbonate/bicarbonate ions in the superoxide-generating reaction of adrenaline autoxidation

Involvement of carbonate/bicarbonate ions in the superoxide-generating reaction of adrenaline autoxidation

Regulation of CuZnSOD and Its Redox Signaling Potential: Implications for Amyotrophic Lateral Sclerosis

Redox control of enzymatic functions: The electronics of life's circuitry

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