Tightly bound oxalacetate and the activation of succinate dehydrogenase

[65] Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods

WILLIAMSON, J. R., & Corkey, B. E. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13072-4 · Cited by 876 · see citing works

Limitations of the Phenazine Methosulphate Assay for Succinic and Related Dehydrogenases

Arrigoni, O., & Singer, T. P. (1962) · Nature · doi:10.1038/1931256a0 · Cited by 375 · see citing works

Batch purification of ovomucoid and characterization of the purified product

Davis, J. G., Mapes, C. J., & Donovan, J. W. (1971) · Biochemistry · doi:10.1021/bi00777a006 · Cited by 270 · see citing works

Succinate dehydrogenase. I. Purification, molecular properties, and substructure

Hatefi, Y., & Davis, K. A. (1971) · Biochemistry · doi:10.1021/bi00789a014 · Cited by 254 · see citing works

STUDIES ON SUCCINIC DEHYDROGENASE

Kearney, E. B. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70623-6 · Cited by 151 · see citing works

Studies on succinate dehydrogenase

Dervartanian, D. V., & Veeger, C. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(64)90182-8 · Cited by 130 · see citing works

[82] Succinic dehydrogenase

Bernath, P., & Singer, T. P. (1962) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(62)05283-0 · Cited by 101 · see citing works

Control of succinate dehydrogenase in mitochondria

Gutman, M., Kearney, E. B., & Singer, T. P. (1971) · Biochemistry · doi:10.1021/bi00801a025 · Cited by 97 · see citing works

Studies on Succinate Dehydrogenase. Site of Attachment of the Covalently-Bound Flavin to the Peptide Chain

Salach, J. I., Walker, W. H., Singer, T. P., Ehrenberg, A., Hemmerich, P. H., Ghisla, S., & Hartmann, U. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb01765.x · Cited by 88 · see citing works

Succinate dehydrogenase. XVIII. Regulation of succinate dehydrogenase activity by reduced coenzyme Q10

Singer, T. P., Gutman, M., & Kearney, E. B. (1971) · Biochemistry · doi:10.1021/bi00790a011 · Cited by 75 · see citing works

Studies on succinate dehydrogenase. II. On the nature of the reaction of competitive inhibitors and substrates with succinate dehydrogenase

Dervartanian, D. V., & Veeger, C. (1965) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/s0926-6593(65)80228-4 · Cited by 40 · see citing works

Studies on succinate dehydrogenase

Zeylemaker, W. P., Klaasse, A. D. M., & Slater, E. C. (1969) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(69)90242-3 · Cited by 35 · see citing works

Regulatory properties of succinate dehydrogenase: Activation by succinyl CoA, pH, and anions

Kearney, E. B., Mayr, M., & Singer, T. P. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(72)80171-2 · Cited by 26 · see citing works

The resolution of some discrepancies concerning the molecular weight and subunit structure of succinate dehydrogenase

Coles, C. J., Tisdale, H. D., Kenney, W. C., & Singer, T. P. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90060-5 · Cited by 14 · see citing works

[61] Separation of citric acid cycle and related compounds by gas chromatography

Alcock, N. W. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13068-2 · Cited by 9 · see citing works

Differential investigation of the capacity of succinate oxidation in human skeletal muscle

Fischer, J., Ruitenbeek, W., BERDEN, J. A., Trijbels, J. M. F., Veerkamp, J. H., Stadhouders, A. M., Sengers, R. C. A., & Janssen, A. J. M. (1985) · Clinica Chimica Acta · doi:10.1016/0009-8981(85)90135-4 · Cited by 471 · see citing works

Determination of the Activity of Succinate, NADH, Choline, and α‐Glycerophosphate Dehydrogenases

Singer, T. P. (1974) · Methods of biochemical analysis · doi:10.1002/9780470110423.ch3 · Cited by 325 · see citing works

[47] Mammalian succinate dehydrogenase

Ackrell, B. A. C., Kearney, E. B., & Singer, T. P. (1978) · Methods in Enzymology · doi:10.1016/s0076-6879(78)53050-4 · Cited by 255 · see citing works

Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning

Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201 · see citing works

Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes

Blaza, J. N., Serreli, R., Jones, A. J. Y., Mohammed, K., & Hirst, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413855111 · Cited by 181 · see citing works

Succinate dehydrogenase (mitochondrial complex II ) is a source of reactive oxygen species in plants and regulates development and stress responses

Messeder, D. J., Caverzan, A., Rauber, R., Ferreira, E. D. S., Margis-Pinheiro, M. M. A. N., & Galina, A. (2015) · New Phytologist · doi:10.1111/nph.13515 · Cited by 158 · see citing works

High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates

Muller, F. L., Liu, Y., Abdul-Ghani, M. A., Lustgarten, M. S., Bhattacharya, A., Jang, Y. C., & Van Remmen, H. (2008) · Biochemical Journal · doi:10.1042/bj20071162 · Cited by 150 · see citing works

Q-site inhibitor induced ROS production of mitochondrial complex II is attenuated by TCA cycle dicarboxylates

Siebels, I., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.06.005 · Cited by 130 · see citing works

The endogenous mitochondrial complex II inhibitor malonate regulates mitochondrial ATP-sensitive potassium channels: implications for ischemic preconditioning

Wojtovich, A. P., & Brookes, P. S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.025 · Cited by 119 · see citing works

Role of Oxalacetate in the Regulation of Mammalian Succinate Dehydrogenase

Ackrell, B. A. C., Kearney, E. B., & Mayr, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42790-7 · Cited by 102 · see citing works

Electron flux through the mitochondrial ubiquinone

Gutman, M. (1980) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(80)90013-0 · Cited by 103 · see citing works

Physiological consequences of complex II inhibition for aging, disease, and the mKATP channel

Wojtovich, A. P., Smith, C. O., Haynes, C. M., Nehrke, K. W., & Brookes, P. S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.007 · Cited by 83 · see citing works

The versatility of plant organic acid metabolism in leaves is underpinned by mitochondrial malate–citrate exchange

Lee, C. P., Elsässer, M., Fuchs, P., Fenske, R., Schwarzländer, M., & Millar, A. H. (2021) · The Plant Cell · doi:10.1093/plcell/koab223 · Cited by 80 · see citing works

Ubiquinone-binding site mutagenesis reveals the role of mitochondrial complex II in cell death initiation

Kluckova, K., Sticha, M., Cerny, J., Mracek, T., Dong, L., Drahota, Z., Gottlieb, E., Neuzil, J., & Rohlena, J. (2015) · Cell Death & Disease · doi:10.1038/cddis.2015.110 · Cited by 66 · see citing works

Modulation of mitochondrial succinate dehydrogenase activity, mechanism and function

Gutman, M. (1978) · Molecular and Cellular Biochemistry · doi:10.1007/bf00229453 · Cited by 66 · see citing works

Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the “oxaloacetate-inhibited” state

Huang, L.-S., Shen, J. T., Wang, A. C., & Berry, E. A. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.06.015 · Cited by 65 · see citing works

Regulation of Succinate Dehyrogenase in Higher Plants

Singer, T. P., Oestreicher, G., Hogue, P., Contreiras, J., & Brandao, I. (1973) · PLANT PHYSIOLOGY · doi:10.1104/pp.52.6.616 · Cited by 64 · see citing works

Differential susceptibility of mitochondrial complex II to inhibition by oxaloacetate in brain and heart

Степанова, А., Shurubor, Y. I., Valsecchi, F., Manfredi, G., & Galkin, A. S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.06.002 · Cited by 57 · see citing works

New Insights into the Regulation of Plant Succinate Dehydrogenase

Affourtit, C., Krab, K., Leach, G., Whitehouse, D. G., & Moore, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103111200 · Cited by 58 · see citing works

Epr studies on the mechanism of action of succinate dehydrogenase in activated preparations

Beinert, H., Ackrell, B. A. C., Kearney, E. B., & Singer, T. P. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80457-2 · Cited by 52 · see citing works

Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase

King, T. E., Ohnishi, T., Winter, D. B., & Wu, J. T. (1976) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-3270-1_15 · Cited by 50 · see citing works

[6] Resolution of complex II and isolation of succinate dehydrogenase (EC 1.3.99.1)

Hatefi, Y. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53009-7 · Cited by 50 · see citing works

Functional and composition differences between mitochondrial complex II in Arabidopsis and rice are correlated with the complex genetic history of the enzyme

Huang, S., Taylor, N. L., Narsai, R., Eubel, H., Whelan, J., & Millar, A. H. (2009) · Plant Molecular Biology · doi:10.1007/s11103-009-9573-z · Cited by 44 · see citing works

Activation of Succinate Dehydrogenase by Anions and pH

Kearney, E. B., Ackrell, B. A. C., Mayr, M., & Singer, T. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42789-0 · Cited by 43 · see citing works

Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles

Hillar, M., Lott, V., & Lennox, B. (1975) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf01558459 · Cited by 40 · see citing works

The reaction of N-ethylmaleimide at the active site of succinate dehydrogenase.

Kenney, W. C. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41598-6 · Cited by 40 · see citing works

The Enzymes and the Enzyme Complexes of the Mitochondrial Oxidative Phosphorylation System

Hatefi, Y., RAGAN, C. I., & Galante, Y. M. (1985) · Springer eBooks · doi:10.1007/978-1-4684-4604-3_1 · Cited by 40 · see citing works

Enzyme promiscuity, metabolite damage, and metabolite damage control systems of the tricarboxylic acid cycle

Niehaus, T. D., & Hillmann, K. B. (2020) · FEBS Journal · doi:10.1111/febs.15284 · Cited by 33 · see citing works

Factors contributing to the inhibition of aspartate aminotransferase by dicarboxylic acids.

Bonsib, S. M., Harruff, R. C., & Jenkins, W. T. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40718-7 · Cited by 33 · see citing works

Succinate is the controller of O 2 − /H2O2 release at mitochondrial complex I : negative modulation by malate, positive by cyanide

Zoccarato, F., Cavallini, L., & Alexandre, A. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9238-2 · Cited by 31 · see citing works

Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activity

Gutman, M., Bonomi, F., Pagani, S., Cerletti, P., & Kroneck, P. M. H. (1980) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(80)90171-1 · Cited by 29 · see citing works

The steady state activity of succinate dehydrogenase in the presence of opposing effectors

Gutman, M., & Silman, N. (1975) · Molecular and Cellular Biochemistry · doi:10.1007/bf01731407 · Cited by 26 · see citing works

The Enzymes and the Enzyme Complexes of the Mitochondrial Oxidative Phosphorylation System

Hatefi, Y. (1976) · Springer eBooks · doi:10.1007/978-1-4899-2693-7_1 · Cited by 25 · see citing works

Reconstitution of photosynthetic electron transport and photophosphorylation in cytochrome-c2-deficient membrane preparation of Rhodopseudomonas capsulata

Hochman, A., & Carmeli, C. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90121-7 · Cited by 25 · see citing works

Oxidation of malate by the mitochondrial succinate–ubiquinone reductase

Belikova, Y. O., Kotlyar, A. B., & Vinogradov, A. D. (1988) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(88)90245-9 · Cited by 23 · see citing works

The effect of opposing effectors on activation level of succinate dehydrogenase: equilibrium and kinetic studies

Gutman, M. (1976) · Biochemistry · doi:10.1021/bi00651a027 · Cited by 19 · see citing works

Tight binding of oxaloacetate to succinate dehydrogenase

Priegnitz, A., Brzhevskaya, O. N., & Wojtczak, L. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90031-4 · Cited by 19 · see citing works

The steady state activity of succinate dehydrogenase in the presence of opposing effectors

Gutman, M., & Silman, N. (1975) · Molecular and Cellular Biochemistry · doi:10.1007/bf01732163 · Cited by 16 · see citing works

Localization of the oxaloacetate-binding site in the iron-flavoprotein subunit of the inhibitor-succinate dehydrogenase complex

Winter, D. B., & King, T. E. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90840-7 · Cited by 16 · see citing works

A universal metabolite repair enzyme removes a strong inhibitor of the TCA cycle

Zmuda, A. J., Kang, X., Wissbroecker, K. B., Saxhaug, K. F., Costa, K. C., Hegeman, A. D., & Niehaus, T. D. (2024) · Nature Communications · doi:10.1038/s41467-024-45134-0 · Cited by 15 · see citing works

A shortcut to mitochondrial signaling and pathology: A commentary on “Nonenzymatic formation of succinate in mitochondria under oxidative stress”

Brookes, P. S., Freeman, R. S., & Barone, M. C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.03.019 · Cited by 13 · see citing works

Regulatory Properties of Perchlorate-extracted Succinate Dehydrogenase

Coles, C. J., Tisdale, H. D., Kenney, W. C., & Singer, T. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43041-x · Cited by 12 · see citing works

Ca2+ Requirement in ATP‐Induced Activation of Uncoupled Oxidation of Succinate in Isolated Rat‐Liver Mitochondria

Ezawa, I., & Ogata, E. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11683.x · Cited by 10 · see citing works

Activation of Succinate Dehydrogenase by FMNH2 and by Photoreduction

Salach, J. I., & Singer, T. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42539-8 · Cited by 9 · see citing works

Factors limiting mitochondrial respiration in media of high solute content

Campbell, L. C., Raison, J. K., & Brady, C. (1975) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf01558547 · Cited by 8 · see citing works

Iron–Sulfur Flavoprotein Dehydrogenases

Singer, T. P., Gutman, M., & Massey, V. (1973) · Elsevier eBooks · doi:10.1016/b978-0-12-456001-7.50013-6 · Cited by 7 · see citing works

Fueling asthma inflammation via bioenergetic metabolic reprogramming

Mulya, A., Janocha, A. J., Novotny, M., Reichard, A., Hamm, E., Chen, R., Mey, J. T., Peterson, L., Mavrakis, L. A., Beck, B., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104160 · Cited by 3 · see citing works

The Arabidopsis mitochondrial dicarboxylate carrier 2 maintains leaf metabolic homeostasis by uniting malate import and citrate exportPreprint

Lee, C. P., Elsässer, M., Fuchs, P., Fenske, R., Schwarzländer, M., & Millar, A. H. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.28.065441 · Cited by 3 · see citing works

Activation of succinate dehydrogenase and the effect of cyanide

Zanetti, G., & Galante, Y. M. (1974) · Cellular and Molecular Life Sciences · doi:10.1007/bf01938334 · Cited by 1 · see citing works

Metabolite Damage and Repair in Health and Disease

Linster, C. L., Veiga‐da‐Cunha, M., Niehaus, T. D., Bommer, G. T., & SCHAFTINGEN, E. V. (2026) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-062024-123639

Oxaloacetate inhibition of succinate dehydrogenase: mechanism and physiological implications

Sivitz, W. I., & Yu, L. P. (2026) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00200.2026

Role of Oxalacetate in the Regulation of Mammalian Succinate Dehydrogenase

Ackrell, B. A. C., Kearney, E. B., & Mayr, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42790-7 · Cited by 102 · see citing works

Studies on Succinate Dehydrogenase

Kimura, T., HAUBER, J., & Singer, T. P. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99466-4 · Cited by 99 · see citing works

Mechanism of the reductive activation of succinate dehydrogenase.

Ackrell, B. A. C., Kearney, E. B., & Edmondson, D. E. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40916-2 · Cited by 54 · see citing works

The steady state activity of succinate dehydrogenase in the presence of opposing effectors

Gutman, M., & Silman, N. (1975) · Molecular and Cellular Biochemistry · doi:10.1007/bf01731407 · Cited by 26 · see citing works

Tight binding of oxaloacetate to succinate dehydrogenase

Priegnitz, A., Brzhevskaya, O. N., & Wojtczak, L. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90031-4 · Cited by 19 · see citing works