Cited by 341Selenium in Biological SystemsRedox biology and oxidative stressGlutathione Transferases and Polymorphisms

The DOI matches its Crossref record; 0 of the 3 references it cites were found in a registry or an index.

Glutathione Peroxidase, V. The kinetic mechanism

Flohé, Leopold, Loschen, Gerriet, Günzler, Wolfgang A., Eichele, Erich·1972·Hoppe-Seyler´s Zeitschrift für physiologische Chemie

DOI 10.1515/bchm2.1972.353.1.987

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1515/bchm2.1972.353.1.987

Cites

0 of 3 references verified0 citation errors · 3 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Chem in Biochem Gue - roult Enzymol / this Biochim
Boivin (1969) · BioL Clin BioL Chem Biochem J Biophys Acta
Unresolved
Using the terminology of Clelandt this mecha - Klin Wochemchr Biochim / Lab Clin
Flohe (1971) · Biophys Acta
Unresolved
Chim Brit
Necheles (1970) · Acta J Haematol
Unresolved

Flagged first, then by citations

Show all 3 references

3 of the 3 references couldn’t be matched to a known paper.

Sorted by citations

Items 101–200 of 341

The labour pains of biochemical selenology: The history of selenoprotein biosynthesis
Flohé, L. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.031 · Cited by 94
Self-citation
The Isolation and Crystal Structure of a Cyclic Selenenate Ester Derived from Bis(2,6‐diformyl‐4‐tert‐butylphenyl)diselenide and its Glutathione Peroxidase‐Like Activity
Zade, S. S., Singh, H. B., & Butcher, R. J. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200460380 · Cited by 92
Effect of Dietary Methionine on the Biopotency of Selenite and Selenomethionine in the Rat
Sunde, R. A., Gutzke, G. E., & Hoekstra, W. G. (1981) · Journal of Nutrition · doi:10.1093/jn/111.1.76 · Cited by 90
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 96
The biochemistry of selenoproteins
Sunde, R. A. (1984) · Journal of the American Oil Chemists Society · doi:10.1007/bf02540827 · Cited by 89
Peroxiredoxins as Preferential Targets in H2O2-Induced Signaling
Randall, L. M., Ferrer‐Sueta, G., & Denicola, A. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405882-8.00003-9 · Cited by 87
Importance of various antioxidant enzymes for cell stability. Confrontation between theoretical and experimental data
Remacle, J., Lambert, D., Raes, M. J., Pigeolet, E., Michiels, C., & Toussaint, O. (1992) · Biochemical Journal · doi:10.1042/bj2860041 · Cited by 85
Semisynthetic Tellurosubtilisin with Glutathione Peroxidase Activity
Mao, S., Dong, Z., Liu, J., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja052451v · Cited by 84
Glutathione Peroxidase: Fact and Fiction
Flohg, L. (2008) · Novartis Foundation symposium · doi:10.1002/9780470715413.ch7 · Cited by 84
The Regulation and Role of Extracellular Glutathione Peroxidase
COMHAIR, S. A. A., & ERZURUM, S. C. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.72 · Cited by 82
A Second Class of Peroxidases Linked to the Trypanothione Metabolism
Hillebrand, H., Schmidt, A., & Krauth‐Siegel, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210392200 · Cited by 83
Biochemistry of Glutathione
Meister, A. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-299257-5.50012-9 · Cited by 83
Hydrogen sulfide inhibits oxidative stress in lungs from allergic mice in vivo
Benetti, L. R., Campos, D., Gurgueira, S. A., Vercesi, A. E., Guedes, C. E. V., Santos, K. L., Wallace, J. L., Teixeira, S. A., Florenzano, J., Costa, S. K. P., et al. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.11.025 · Cited by 82
Biochemistry of selenium: A brief overview
Reddy, C. C., & Massaro, E. J. (1983) · Fundamental and Applied Toxicology · doi:10.1016/s0272-0590(83)80017-7 · Cited by 81
Responses of mitochondrial superoxide dismutase, catalase and glutathione peroxidase activities to aging
Nohl, H., HEGNER, D., & Summer, K. (1979) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(79)90050-2 · Cited by 81
The impact of thiol peroxidases on redox regulation
Flohé, L. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1046858 · Cited by 82
Self-citation
The role of free radicals and antioxidants: How do we know that they are working?
Thomas, M. J. (1995) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399509527683 · Cited by 80
Incorporation of Tellurocysteine into Glutathione Transferase Generates High Glutathione Peroxidase Efficiency
Liu, X., Silks, L. A. “., III, Liu, C., et al. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805365 · Cited by 78
Catalase Activity and Post-anoxic Injury in Monocotyledonous Species
Monk, L. S., Braendle, R., & Crawford, R. M. M. (1987) · Journal of Experimental Botany · doi:10.1093/jxb/38.2.233 · Cited by 77
Looking Back at the Early Stages of Redox Biology
Flohé, L. (2020) · Antioxidants · doi:10.3390/antiox9121254 · Cited by 78
“This enzyme proved not to belong to the GPx family, but is a B-type GSH-S-transferase [111].”
BackgroundResultInfluentialSelf-citation
Blood selenium and glutathione peroxidase activity of populations in New Zealand, Oregon, and South Dakota 1
Whanger, P. D., Beilstein, M. A., Thomson, G. D., Robinson, M. F., & Howe, M. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.14.3181654 · Cited by 74
Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic
Ding, L., Liu, Z., Zhenqi, Z., et al. (1998) · Biochemical Journal · doi:10.1042/bj3320251 · Cited by 73
The Trypanothione System
Krauth‐Siegel, L., Comini, M. A., & Schlecker, T. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-6051-9_11 · Cited by 72
“2) but significantly lower than those of the mammalian seleno-enzymes (> 107 M−1 s−1; Flohé et al., 1972; Hofmann et al., 2002; Flohé and BrigeliusFlohé, 2001).”
Background
A bis-cyclodextrin diselenide with glutathione peroxidase-like activity
LIU, J., Luo, G., Ren, X., et al. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00130-8 · Cited by 72
PHGPx and phospholipase A2/GPx: Comparative importance on the reduction of hydroperoxides in rat liver mitochondria
Antunes, F., Salvador, A., & Pinto, R. E. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00040-5 · Cited by 70
Hydrogen peroxide metabolism and sensing in human erythrocytes: A validated kinetic model and reappraisal of the role of peroxiredoxin II
Benfeitas, R., Selvaggio, G., Antunes, F., Coelho, P. M. B. M., & Salvador, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.06.007 · Cited by 74
“[29] for bovine GPx1 fits the time series obtained by Mueller et al.”
Peroxide dependence of the semisynthetic enzyme selenosubtilisin
Bell, I. M., & Hilvert, D. (1993) · Biochemistry · doi:10.1021/bi00213a029 · Cited by 69
Intracellular Glutathione Peroxidases — Structure, Regulation, and Function
Sunde, R. A. (1994) · Springer eBooks · doi:10.1007/978-1-4612-2592-8_4 · Cited by 74
Chelate Ring Size Effect on the Reactivity of [2-(2-Phenyl-5,6-dihydro-4H-1,3-oxazinyl)]lithium and Se···N Interactions in Low-Valent Organoselenium Compounds: Facile Isolation of Diorganotriselenide
Kumar, S., Kandasamy, K., Singh, H. B., et al. (2004) · Organometallics · doi:10.1021/om049722f · Cited by 68
Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3‐phosphate dehydrogenase reveals a peroxidase activity
Boschi‐Müller, S., Müller, S., DORSSELAER, A. V., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01377-5 · Cited by 68
In Vivo Antioxidant Role of Glutathione Peroxidase: Evidence from Knockout Mice
Lei, X. G. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)47021-8 · Cited by 67
Purification and properties of glutathione peroxidase from human placenta
Awasthi, S., Dao, D. D., Lal, A., et al. (1979) · Biochemical Journal · doi:10.1042/bj1770471 · Cited by 66
Purification and characterization of selenium-glutathione peroxidase from hamster liver
Chaudière, J., & Tappel, A. L. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90314-4 · Cited by 65
Smart microgel catalyst with modulatory glutathione peroxidase activity
Huang, X., Yin, Y., Tang, Y. F., et al. (2009) · Soft Matter · doi:10.1039/b816888a · Cited by 64
Mechanism for suppression of cellular biosynthesis of prostaglandins
Cook, H. W., & Lands, W. E. M. (1976) · Nature · doi:10.1038/260630a0 · Cited by 64
Some Selenium‐Dependent Biochemical Processes
Stadtman, T. C. (1979) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122938.ch1 · Cited by 62
Advances in antioxidant nanozymes for biomedical applications
Liu, X., Xu, H., Peng, H., Wan, L., Di, D., Qin, Z., He, L., Lu, J., Wang, S., & Zhao, Q. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215610 · Cited by 61
Selenium-Mediated Micellar Catalyst: An Efficient Enzyme Model for Glutathione Peroxidase-like Catalysis
Huang, X., Dong, Z., Liu, J., Mao, S., Xu, J., Luo, G., & Shen, J. (2006) · Langmuir · doi:10.1021/la061727p · Cited by 59
Age-related changes in arachidonic acid peroxidation and glutathione-peroxidase activity in human platelets
Véricel, E., Rey, C., Calzada, C., Haond, P., Chapuy, P., & Lagarde, M. (1992) · Prostaglandins · doi:10.1016/0090-6980(92)90067-4 · Cited by 59
In vivo speciation studies and antioxidant properties of bromine in Laminaria digitata reinforce the significance of iodine accumulation for kelps
Küpper, F. C., Carpenter, L. J., Leblanc, C., Toyama, C., Uchida, Y., Maskrey, B. H., Robinson, J., Verhaeghe, E., Malin, G., Luther, G. W., et al. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ert110 · Cited by 61
Peroxiredoxins in antioxidant defense and redox regulation
Flohé, L., Budde, H., & Hofmann, B. (2003) · BioFactors · doi:10.1002/biof.5520190102 · Cited by 58
Self-citation
Estimation of Individual Types of Glutathione Peroxidases
Brigelius‐Flohé, R., Wingler, K., & Müller, C. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)47011-5 · Cited by 58
50 Years of Organoselenium Chemistry, Biochemistry and Reactivity: Mechanistic Understanding, Successful and Controversial Stories
Madabeni, A., Bortoli, M., Nogara, P. A., Ribaudo, G., Tiezza, M. D., Flohé, L., da Rocha, J. B. T., & Orian, L. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202403003 · Cited by 62
Self-citation
Sensitive fluorometric assays for glutathione peroxidase and reductase
Weiss, C., Maker, H. S., & Lehrer, G. M. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90556-4 · Cited by 57
Density Functional Theory Study of the Reaction Mechanism and Energetics of the Reduction of Hydrogen Peroxide by Ebselen, Ebselen Diselenide, and Ebselen Selenol
Pearson, J. K., & Boyd, R. J. (2007) · The Journal of Physical Chemistry A · doi:10.1021/jp071499n · Cited by 56
Glutathione peroxidase-like nanozymes: mechanism, classification, and bioapplication
Lai, Y., Wang, J., Yue, N., Zhang, Q., Wu, J., Qi, W. D., & Su, R. (2023) · Biomaterials Science · doi:10.1039/d2bm01915a · Cited by 59
Internally stabilized selenocysteine derivatives: syntheses, 77Se NMR and biomimetic studies
Phadnis, P. P., & Mugesh, G. (2005) · Organic & Biomolecular Chemistry · doi:10.1039/b505299h · Cited by 56
β-Amyloid Peptides Are Cytotoxic to Astrocytes in Culture: A Role for Oxidative Stress
Brera, B., Serrano, A., & CEBALLOS, M. L. D. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0313 · Cited by 55
Artificial Imitation of Glutathione Peroxidase with 6-Selenium-Bridged β-Cyclodextrin
Liu, J., Gao, S., Luo, G., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8545 · Cited by 55
Cytosolic glutathione peroxidase from liver of pacu (Piaractus mesopotamicus), a hypoxia-tolerant fish of the Pantanal
Bastos, V. L. F. C., de Salles, J. B., Valente, R. H., León, I. R., Perales, J., Dantas, R. F., Albano, R. M., Bastos, F. F., & Bastos, J. C. (2007) · Biochimie · doi:10.1016/j.biochi.2007.04.003 · Cited by 55
Glutathione peroxidase 1-deficient mice are more susceptible to doxorubicin-induced cardiotoxicity
Gao, J., Xiong, Y., Ho, Y.-S., Liu, X., Chua, C. C., Xu, X., Wang, H., Hamdy, R. C., & Chua, B. H. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.05.027 · Cited by 54
“The location and low Km of Gpx1 for H2O2 may facilitate its ability to detoxify the H2O2 that is generated in the mitochondria of heart following DOX treatment (16,17).”
Background
Longitudinal selenium status in healthy British adults: assessment using biochemical and molecular biomarkers
Sunde, R. A., Paterson, E., Evenson, J. K., Barnes, K. M., Lovegrove, J. A., & Gordon, M. H. (2008) · British Journal Of Nutrition · doi:10.1017/s0007114508006831 · Cited by 54
“It is difficult to compare Gpx enzyme activities directly between studies due to differences in assay conditions, especially because Gpx activity is dependent on assay GSH concentration((57)).”
Catalytic antioxidant therapy by metallodrugs: lessons from metallocorroles
Haber, A., & Gross, Z. (2015) · Chemical Communications · doi:10.1039/c4cc08715a · Cited by 53
Selenoglutaredoxin as a Glutathione Peroxidase Mimic
Casi, G., Roelfes, G., & Hilvert, D. (2008) · ChemBioChem · doi:10.1002/cbic.200700745 · Cited by 51
Development of an amperometric assay for the determination of reduced glutathione, using glutathione peroxidase and screen‐printed carbon electrodes chemically modified with cobalt phthalocyanine
Wring, S. A., Hart, J. P., & Birch, B. J. (1992) · Electroanalysis · doi:10.1002/elan.1140040307 · Cited by 51
Impaired Glutathione Peroxidase Activity Accounts for the Age-Related Accumulation of Hydrogen Peroxide in Activated Human Neutrophils
Ito, Y., Kajkenova, O., Feuers, R. J., et al. (1998) · The Journals of Gerontology Series A · doi:10.1093/gerona/53a.3.m169 · Cited by 50
“The reaction mechanism for glutathione peroxidase is "ping pong," where a product (H2O) is released between the addition of two substrates, H2O2 and GSH (20).”
Background
Synthesis, characterization and structures of 2-(3,5-dimethylpyrazol-1-yl)ethylseleno derivatives and their probable glutathione peroxidase (GPx) like activity
Hodage, A. S., Phadnis, P. P., Wadawale, A., et al. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00807a · Cited by 50
The biomedical applications of nanozymes in orthopaedics based on regulating reactive oxygen species
Gao, X., Zhang, J., Gong, Y., & Yan, L. W. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02844-3 · Cited by 56
“…catalytic process of GPx-like nanozymes involves the reduction of H 2 O 2 and organic hydroper-oxides in the presence of reduced GSH. Similar to natu-ral GPx, most GPx-like nanozymes follow a ping-pong mechanism [45], where hydroperoxide oxidizes their active sites to form peroxide intermediates.”
Background
The Rapid‐Flow‐Quench Method in the Study of Fast Reactions in Biochemistry: Extension to Subzero Conditions
Barman, T. E., & Travers, F. (1985) · Methods of biochemical analysis · doi:10.1002/9780470110522.ch1 · Cited by 49
The applications of nanozymes in neurological diseases: From mechanism to design
Zhang, Y., Zhang, L., Wang, M., & Li, P. (2023) · Theranostics · doi:10.7150/thno.83370 · Cited by 50
“To date, studies have shown that GPx-like nanozymes have two catalytic mechanisms, that is, ping-pong and ordered mechanisms [24, 25].”
Background
Selenoproteins of the glutathione system
Flohé, L., & Brigelius‐Flohé, R. (2007) · Springer eBooks · doi:10.1007/0-387-33827-6_15 · Cited by 48
Self-citation
Rat liver cytosolic glutathione peroxidase: Reactivity with linoleic acid hydroperoxide and cumene hydroperoxide
Forstrom, J. W., Stults, F. H., & Tappel, A. L. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90007-9 · Cited by 48
A Novel Glutathione Peroxidase Mimic with Antioxidant Activity
Ren, X., Yang, L., Liu, J., et al. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2238 · Cited by 47
Some chemical and biochemical constraints of oxidative stress in living cells* *This chapter is dedicated to René Buvet († November 26, 1992) who led me to the astonishing world of oxygen biochemistry.
Chaudière, J. (1994) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60438-x · Cited by 46
The Non-flavin Redox Center of the Streptococcal NADH Peroxidase
Poole, L. B., & Claiborne, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63861-x · Cited by 46
Heterologous Expression and Enzymatic Properties of a Selenium-independent Glutathione Peroxidase from the Parasitic Nematode Brugia pahangi
Tang, L., Gounaris, K., Griffiths, C. M., & Selkirk, M. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.31.18313 · Cited by 45
A modulatory bifunctional artificial enzyme with both SOD and GPx activities based on a smart star-shaped pseudo-block copolymer
Yu, S., Yin, Y., Zhu, J., Huang, X., Luo, Q., Xu, J., Shen, J., & Liu, J. (2010) · Soft Matter · doi:10.1039/c0sm00162g · Cited by 45
Antihyperlipidemic and Antioxidant Effects of Averrhoa Carambola Extract in High-Fat Diet-Fed Rats
Aladaileh, S. H., Saghir, S. A. M., Murugesu, K., et al. (2019) · Biomedicines · doi:10.3390/biomedicines7030072 · Cited by 45
“Thiobarbituric acid reactive substances (TBARS) [29], reduced glutathione (GSH) [30], superoxide dismutase (SOD) [31], glutathione peroxidase (GPX) [32], and catalase (CAT) [33] were determined in the liver homogenate.”
Background
Emerging roles for non-selenium containing ER-resident glutathione peroxidases in cell signaling and disease
Buday, K., & Conrad, M. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0286 · Cited by 48
“Kinetic studies on GPX1, and later on GPX3 and GPX4, revealed that SecGPXs have an extremely high rate constant for the reaction with the hydroperoxide (Flohe et al. 1972; Takebe et al. 2002).”
Background
Hydrogen Peroxide-Forming NADH Oxidase Belonging to the Peroxiredoxin Oxidoreductase Family: Existence and Physiological Role in Bacteria
Nishiyama, Y., Massey, V., Takeda, K., et al. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.8.2431-2438.2001 · Cited by 45
Block Copolymer Micelles as Matrixes for Incorporating Diselenide Compounds: A Model System for a Water-Soluble Glutathione Peroxidase Mimic Fine-Tuned by Ionic Strength
Wang, Y., Xu, H., Ma, N., Wang, Z., Zhang, X., Liu, J., & Shen, J. (2006) · Langmuir · doi:10.1021/la060711w · Cited by 44
Selenium-Catalyzed Reduction of Hydroperoxides in Chemistry and Biology
Orian, L., & Flohé, L. (2021) · Antioxidants · doi:10.3390/antiox10101560 · Cited by 44
“of the enzyme by H2O2 (ca 108 M−1s−1 for bovine GPx1 [30]; more values are compiled in [60]).”
BackgroundInfluentialSelf-citation
Peroxidase: A Term of Many Meanings
Flohé, L., & Ursini, F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2059 · Cited by 42
“Therefore, additional effects such as proton shuttling and polarization of the peroxide bond have to be considered to account for the enzymatic rate constants in the range of 105–107 (78) or 108 M 1 s 1 in the case of the seleno-enzymes (26).”
Self-citation
Emerging perspectives on cytoglobin, beyond NO dioxygenase and peroxidase
Mathai, C., Jourd’heuil, F. L., Lopez‐Soler, R. I., & Jourd’heuil, D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101468 · Cited by 42
Bioimprinted protein exhibits glutathione peroxidase activity
Liu, J., Zhang, K., Ren, X., et al. (2003) · Analytica Chimica Acta · doi:10.1016/s0003-2670(03)00763-3 · Cited by 42
H2O2 Delivery to Cells
Marinho, H. S., Cyrne, L., Cadenas, E., et al. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00010-7 · Cited by 42
Selenium-containing 15-Mer Peptides with High Glutathione Peroxidase-like Activity
Sun, Y., Li, T., Chen, H., Zhang, K., Zheng, K., Mu, Y., Yan, G., Li, W., Shen, J., & Luo, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403032200 · Cited by 42
Brain Insulin Resistance: Focus on Insulin Receptor-Mitochondria Interactions
Анатольевич, П. И., & Pinelis, V. G. (2021) · Life · doi:10.3390/life11030262 · Cited by 43
“Glutathione peroxidase (Gpx1) is a highly effective scavenger for H2O2, with a second-order rate constant of about 107 M-1 s-1 [74].”
Background
Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response
Claiborne, A., Ross, R. P., & Parsonage, D. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90263-9 · Cited by 38
Kinetic modeling of H2O2 dynamics in the mitochondria of HeLa cells
Stein, K. T., Moon, S. J., Nguyen, A. N., & Sikes, H. D. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008202 · Cited by 35
“Reaction Parameter Generation of H2O2 by OxPhos k1 = 4 μM/s [16,40] k2[Gpx1red][H2O2] k2 = 60 μMs [35,41] k3[Gpx1ox][GSH] k3 = 0.”
Identification of the Dehydroascorbic Acid Reductase and Thioltransferase (Glutaredoxin) Activities of Bovine Erythrocyte Glutathione Peroxidase
Washburn, M. P., & Wells, W. W. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0508 · Cited by 37
Inhibition of Erythrocyte Selenium-Glutathione Peroxidase by Auranofin Analogues and Metabolites
Roberts, J. R., & Shaw, C. F. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00634-5 · Cited by 37
Modeling the Reduction of Hydrogen Peroxide by Glutathione Peroxidase Mimics
Pearson, J. K., & Boyd, R. J. (2006) · The Journal of Physical Chemistry A · doi:10.1021/jp0615196 · Cited by 37
A novel nanozyme based on selenopeptide-modified gold nanoparticles with a tunable glutathione peroxidase activity
Zhang, D., Shen, N., Zhang, J., Zhu, J., Guo, Y., & Xu, L. (2020) · RSC Advances · doi:10.1039/c9ra10262k · Cited by 37
An Evaluation of Various Computational Methods for the Treatment of Organoselenium Compounds
Pearson, J. K., Ban, F., & Boyd, R. J. (2005) · The Journal of Physical Chemistry A · doi:10.1021/jp054185d · Cited by 36
Plasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins
Djuika, C. F., Fiedler, S., Schnölzer, M., Sanchez, C. P., Lanzer, M., & Deponte, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.020 · Cited by 36
Reaction Mechanism of Amphibacillus xylanus NADH Oxidase/Alkyl Hydroperoxide Reductase Flavoprotein
Niimura, Y., & Massey, V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30459 · Cited by 36
Idiosyncratic Reactions: New Methods of Identifying High‐risk Patients
Glauser, T. A. (2000) · Epilepsia · doi:10.1111/j.1528-1157.2000.tb02943.x · Cited by 35
Redox control of GPx catalytic activity through mediating self-assembly of Fmoc-phenylalanine selenide into switchable supramolecular architectures
Huang, Z., Luo, Q., Guan, S., et al. (2014) · Soft Matter · doi:10.1039/c4sm02030h · Cited by 33
Thiol-dependent peroxidases care little about homology-based assignments of function
Flohé, L., Jaeger, T., Pilawa, S., & Sztajer, H. (2003) · Redox Report · doi:10.1179/135100003225002862 · Cited by 33
“The debate over whether it could compete with catalase in H 2 O 2 metabolism was settled by working out second order rate constants beyond 10(7) Ms for the reaction with various hydroperoxides.(16,17) In the early 1970s, GPx-1 became the first selenoprotein to be discovered in mammals,(18) whereby the extreme reaction…”
BackgroundSelf-citation
Construction of the Active Site of Glutathione Peroxidase on Polymer-Based Nanoparticles
Huang, X., Liu, Y., Liang, K., et al. (2008) · Biomacromolecules · doi:10.1021/bm701386b · Cited by 33
Different effects of Triton X-100, deoxycholate, and fatty acids on the kinetics of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase
Maiorino, M., Roveri, A., Gregolin, C., & Ursini, F. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90369-3 · Cited by 32
Kinetic studies on the hydrogen peroxide elimination by cultured PC12 cells: rate limitation by glucose-6-phosphate dehydrogenase
Hashida, K., Sakakura, Y., & Makino, N. (2002) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00282-9 · Cited by 32
Incorporation of glutathione peroxidase active site into polymer based on imprinting strategy
Huang, X., Yin, Y., Liu, Y., et al. (2009) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2009.01.033 · Cited by 31
Tellurium‐Based Polymeric Surfactants as a Novel Seleno‐Enzyme Model with High Activity
Huang, X., Dong, Z., Liu, J., et al. (2006) · Macromolecular Rapid Communications · doi:10.1002/marc.200600468 · Cited by 31
Selenoproteins of the glutathione system
Flohé, L., & Brigelius‐Flohé, R. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_14 · Cited by 31
Self-citation
A dual attack on the peroxide bond. The common principle of peroxidatic cysteine or selenocysteine residues
Tiezza, M. D., Bickelhaupt, F. M., Flohé, L., Maiorino, M., Ursini, F., & Orian, L. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101540 · Cited by 30
Self-citation
A novel dicyclodextrinyl diselenide compound with glutathione peroxidase activity
Lv, S., Wang, X., Mu, Y., Zang, T., Ji, Y., Liu, J., Shen, J., & Luo, G. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05913.x · Cited by 30
ROLE OF GSH PEROXIDASE IN LIPID PEROXIDE METABOLISM
Flohé, L. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-768050-7.50015-9 · Cited by 30
Self-citation
Construction of a smart temperature-responsive GPx mimic based on the self-assembly of supra-amphiphiles
Zou, H., Sun, H., Wang, L., et al. (2015) · Soft Matter · doi:10.1039/c5sm02074c · Cited by 29

Authors: Flohé, L., Loschen, G., Günzler, W. A., & Eichele, E.
ORCID: Flohé, Leopold
Venue: Hoppe-Seyler´s Zeitschrift für physiologische Chemie
Publisher: Walter de Gruyter GmbH
Published: 1972-01
Volume: 353
Issue: 1
Pages: 987-1000
ISSN: 0018-4888 (ISSN-L)
DOI: 10.1515/bchm2.1972.353.1.987
OpenAlex: W2002449018
Cited by: 340
References: 3
Citations by year: 2025: 4 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 5 · 2020: 11 · 2019: 5 · 2018: 3 · 2017: 6 · 2016: 4 · 2015: 10 · 2014: 13 · 2013: 11 · 2012: 6
FWCI: 4.47
Type: journal article
Language: en
Open access: closed
Locations: Hoppe-Seyler´s Zeitschrift für physiologische Chemie (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: glutathione peroxidase, enzyme kinetics, kinetic mechanism, hydrogen peroxide reduction, glutathione
MeSH terms: Animals, Cattle, Chemistry, Physical, Coumarins, Enzyme Activation, Glutathione, Hydrogen-Ion Concentration, Kinetics, Mathematics, Oxidation-Reduction, Peroxidases, Peroxides, Polarography, Spectrophotometry, Sulfates, Sulfhydryl Compounds, Titanium

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Glutathione Peroxidase, V. The kinetic mechanism

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks