Reactive Oxygen Intermediates in Biochemistry

Naqui, Ali; Chance, Britton; Cadenas, Enrique

doi:10.1146/annurev.bi.55.070186.001033

Cited by 223 publications

(82 citation statements)

References 88 publications

(142 reference statements)

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“…It is known that two to four percent of the total oxygen consumed by the mitochondria undergoes one electron reduction with the production of a superoxide radical, consequently producing hydrogen peroxide [37]. Secondary muscle degradation following a single bout of intense and acute exercise induces oxidative stress in muscle [14]; however, the effect of exercise-induced muscle damage on oxidative stress in circulating blood has not been studied extensively.…”

Section: Discussionmentioning

confidence: 99%

Effects of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis

Park

Man-Gyoon

2015

J. Exerc. Nutr, Biochem.

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Kyung-Shin Park and Man-Gyoon Lee. Effects of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis. JENB., Vol. 19, No. 2, pp.55-63, 2015 [Purpose] The purpose of this study was to investigate the effect of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis.[Methods] Thirteen moderately trained male subjects performed three 40 min treadmill runs at ~70% VO2max on separate days: a level run (L) followed by two downhill runs (DH1 and DH2). Blood samples were taken at rest (PRE) and immediately (POST), 2 h, 24 h, and 48 h after each run. Data were analyzed using 2-way repeated measures ANOVA with post hoc Tukey tests.[Results] Creatine kinase (CK) activity and oxidative stress level were significantly elevated at 24 h and 48 h following DH1 (P < 0.05). The level of oxidative stress at the POST measurement following DH1 and DH2 was greater than PRE. The rate of leukocyte apoptosis was significantly increased at the POST measurement following all three runs, and remained elevated for up to 48 h following DH1 (P < 0.01).[Conclusion] CK activity and oxidative stress were elevated following an acute bout of moderate intensity downhill running, resulting in a greater apoptotic response at 24 h and 48 h post-exercise in comparison with level grade running or a second downhill run. These elevations were blunted following DH2. Although the link between exercise-induced muscle damage and leukocyte apoptosis is currently unknown, the differential response to DH1 vs. L and DH2 indicates that it may be mediated by the elevation of oxidative stress.

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Section: Discussionmentioning

confidence: 99%

Effects of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis

Park

Man-Gyoon

2015

J. Exerc. Nutr, Biochem.

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“…and H 2 O 2 formation are less well understood. Molecular oxygen is a triplet species that can only accept electrons one at a time from potential donors (14). This restriction ensures that oxygen does not spontaneously oxidize most reduced biomolecules, such as NAD(P)H, which are obligate two-electron donors.…”

Section: Waysmentioning

confidence: 99%

Mechanism of Superoxide and Hydrogen Peroxide Formation by Fumarate Reductase, Succinate Dehydrogenase, and Aspartate Oxidase

Messner

Imlay

2002

Journal of Biological Chemistry

260

227

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Superoxide dismutases, catalases, and peroxidases are ubiquitous among aerobic and aerotolerant organisms, suggesting that their substrates, superoxide and hydrogen peroxide, are inevitable toxic by-products of aerobic metabolism (1, 2). Considerable progress has been made in identifying the mechanisms by which these species damage cells (2-11). In aerobic environments, mutant organisms that cannot scavenge endogenous O 2. and H 2 O 2 typically grow poorly or die, indicating that these species are formed in potentially toxic doses inside living cells (12, 13). Similar toxicity occurs in wild-type organisms when they are exposed to higher-than-usual levels of oxygen, evidently because these species are formed at elevated rates. Despite this progress, the mechanisms of O 2 . and H 2 O 2 formation are less well understood. Molecular oxygen is a triplet species that can only accept electrons one at a time from potential donors (14). This restriction ensures that oxygen does not spontaneously oxidize most reduced biomolecules, such as NAD(P)H, which are obligate two-electron donors. Instead, enzymes that are competent univalent electron donors are the most likely effectors of inadvertent oxygen reduction. Such enzymes are prominent in electron transport chains. Accordingly, studies in Escherichia coli determined that NADH dehydrogenase II, succinate dehydrogenase, sulfite reductase, and fumarate reductase each formed O 2. and H 2 O 2 when the reduced enzymes were exposed to oxygen (15, 16). These autoxidizing enzymes contain flavins and either iron-sulfur clusters or quinones, all of which are competent at univalent redox reactions. However, in each case the flavin appeared to be the primary site of electron transfer to oxygen. This trend has been noted in other autoxidizing enzymes as well. This may be due to the solvent accessibility of the flavins, which are situated at the protein surface in order to interact with soluble substrates. In contrast, the iron-sulfur clusters are typically buried within polypeptide, and quinones may be sequestered in hydrophobic regions of the proteinmembrane interface where O 2 . formation is disfavored. Interestingly, the rates at which flavoenzymes leak electrons to oxygen vary over several orders of magnitude (15,(17)(18)(19), indicating that additional factors must govern turnover number. We are hopeful that some of these factors might be revealed by study of members of the succinate dehydrogenase/ fumarate reductase family (Fig. 1). These enzymes are structurally and functionally similar to one another (20 -22), and each autoxidizes, albeit at different rates. Succinate dehydrogenase (Sdh), 1 a primary respiratory dehydrogenase, catalyzes electron transfer from succinate to membrane-bound quinone. Fumarate reductase (Frd) catalyzes the opposite reaction in its service as a terminal oxidase during the anaerobic growth of some bacteria and eukarya. The physical structure of the E. coli fumarate reductase has been determined (23), and the pathways of electron movement through both ...

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“…Fax: (1) (919) 613-8177. E-mail: jsiedow@acpub.duke.edu coupled transition metal center, by analogy with other known water-forming oxidases [10]. Previous metal analyses of partially purified alternative oxidase preparations have been inconclusive; Fe, Cu and Mn have each been reported in varying amounts [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center

1995

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The cyanide-resistant, alternative oxidase of plant mitochondria catalyzes the four-electron reduction of oxygen to water, but the nature of the catalytic center associated with this oxidase has yet to be elucidated. We have identified conserved amino acids, including two copies of the iron-binding motif GIu-X-X-His, in the carboxy-terminal hydrophilic domain of the alternative oxidase that suggest the presence of a hydroxo-bridged binuclear iron center, analogous to that found in the enzyme methane monooxygenase. Using the known three-dimensional structures of other binuclear iron proteins, we have developed a structural model for the proposed catalytic site of the alternative oxidase based on these amino acid sequence similarities.

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Reactive Oxygen Intermediates in Biochemistry

Cited by 223 publications

References 88 publications

Effects of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis

Effects of unaccustomed downhill running on muscle damage, oxidative stress, and leukocyte apoptosis

Mechanism of Superoxide and Hydrogen Peroxide Formation by Fumarate Reductase, Succinate Dehydrogenase, and Aspartate Oxidase

The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center

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