The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Dependence of H2O2 Formation by Rat Heart Mitochondria on Substrate Availability and Donor Age
Abstract
We have examined the substrate specificity and inhibitor sensitivity of H2O2 formation by rat heart mitochondria. Active H2O2 production requires both a high fractional reduction of Complex I (indexed by NADH/NAD+ + NADH ratio) and a high membrane potential, delta psi. These conditions are achieved with supraphysiological concentrations of succinate. With physiological concentrations of NAD-linked substrates, rates of H2O2 formation are much lower (less than 0.1% of respiratory chain electron flux) but may be stimulated by the Complex III inhibitor antimycin A, but not by myxothiazol. Addition of Mn2+ to give 10 nmol/mg of mitochondrial protein enhances H2O2 production with all substrate combinations, possibly by repleting mitochondrial superoxide dismutase with this cation. Contrary to previously published work, no increased activity of H2O2 production was found with heart mitochondria from senescent (24 month) rats, relative to young adults (6 month).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Δψm is an important factor for maintaining cellular energy homeostasis, and small reductions in Δψm induced by mild uncoupling were shown to decrease H2O2 emissions (51,52) and produce a natural antioxidant effect (53).”
From TFAM Enhances Fat Oxidation and Attenuates High-Fat Diet–Induced Insulin Resistance in Skeletal Muscle (2019) · cites this paper as [51]
Citations
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Oxidants, antioxidants, and the degenerative diseases of aging.
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055
Mechanisms by which mitochondria transport calcium
Gunter, T. E., & Pfeiffer, D. R. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.258.5.c755 · Cited by 1,640
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214
Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases
Linnane, A., Ozawa, T., Marzuki, S., & Tanaka, M. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92145-4 · Cited by 983
Cited by
Items 401–447 of 447
Chandran, N. A., Kannan, M., Chandrasekaran, S., & Christyraj, J. R. S. S. (2026) · Springer eBooks · doi:10.1007/978-981-96-9670-3_10 · Cited by 2
Understanding how honey bee flight and senescence are connected through oxidative stress (880.1)
Margotta, J. W., Elekonich, M. M., & Roberts, S. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.880.1 · Cited by 1
“Although the exact mechanisms of ROS generation by mitochondria are not fully understood, most studies suggest the major sites of ROS generation in animals are Complex I and Complex III of the electron transport chain (Turrens, 1997; Hansford et al., 1997; Herrero and Barja, 1997; Barja, 1999).”
BackgroundConformation and ion transport of neuronal uncoupling proteins: UCP2, UCP4, and UCP5
Hoang, T. A. (2011) · Scholars Commons (Wilfrid Laurier University) · Cited by 1
Mitochondrial Supercomplexes and ROS Regulation: Implications for Ageing
Genova, M. L., & Lenaz, G. (2015) · CRC Press eBooks · doi:10.1201/b19087-6 · Cited by 2
Dolai, D., Tripathy, S., Dey, S. K., & Roy, S. (2016) · International Journal of Pharma and Bio Sciences · Cited by 1
Oxidative Stress in Cell Signaling and Cell Fate Determination Under Glucose Starvation
Ren, Y., Cheong, C., & Shen, H. (2021) · Springer eBooks · doi:10.1007/978-981-16-0522-2_13 · Cited by 1
Selective striatal cell loss is ameliorated by regulated autophagy of the cortex
Cho, K., & Kim, G. W. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119822 · Cited by 1
Almutairi, B. O., Almutairi, S. M., & Alarifi, S. A. (2024) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2024.103101 · Cited by 1
Golden, T. R., Morten, K., Johnson, F., Samper, E., & Melov, S. (2005) · Elsevier eBooks · doi:10.1016/b978-012088387-5/50008-x · Cited by 1
The NADH-Oxidase Activity of Mitochondria under Hypotony with Respiratory Chain Inhibitors
Lvov, A. M., & Vekshin, N. L. (2019) · BIOPHYSICS · doi:10.1134/s0006350919060137 · Cited by 1
Turnbull, D. M., & Barron, M. J. (2002) · Springer eBooks · doi:10.1007/978-2-8178-0929-8_5 · Cited by 1
Chapter 11 Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis
(2003) · Blue books of practical neurology · doi:10.1016/s1877-3419(09)70112-6 · Cited by 1
Григорьевич, Ш. А., Шугаева, Н. А., Lashtabega, D. A., & Vyskrebentseva, Ė. I. (2010) · Russian Journal of Plant Physiology · doi:10.1134/s1021443710020056 · Cited by 1
ALEXEYEV, M. F., LeDoux, S. P., & Wilson, G. L. (2006) · Elsevier eBooks · doi:10.1016/b978-012369391-4/50042-4 · Cited by 1
Edgar, D., & Trifunović, A. (2007) · Springer eBooks · doi:10.1007/978-88-470-0376-7_7
Sanz, A., Gredilla, R., Herrero, A., & de Quiroga, G. B. (2004) · Revista Española de Geriatría y Gerontología · doi:10.1016/s0211-139x(04)74928-8
Participação da mitocôndria na regulação da viabilidade celular.
Kowaltowski, A. J. (2007) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2007.tde-08102007-145540
“- pela coenzima Q (Turrens et al., 1985; Dawson, 1993; Hansford et al., 1997; Turrens, 1997; Kowaltowski et al., 1998; Starkov e Fiskum, 2001).”
Roe, M. R. (2010) · University of Minnesota Digital Conservancy (University of Minnesota)
Oxygen toxicity and mitochondrial metabolism.
Li, J. (2003) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/822
Diabetic cardiomyopathy: effects of fatty acids and glucose on adult rat cardiac cells
Dyntar, D. (2003) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-004622246
Metabolism of Superoxide Radicals and Hydrogen Peroxide in Mitochondria
Marinho, H. S., & Antunes, F. (2015) · Oxidative stress and disease · doi:10.1201/b19420-3
Arnhold, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816388-7.00004-8
Red-Ox Reactions with NADH Dehydrogenase
Vekshin, N. L. (2019) · Springer eBooks · doi:10.1007/978-3-030-33853-4_6
The role of Banf1 in mechanisms of cellular ageing and cancer prognosis
Plowman, J. (2024) · Queensland University of Technology · doi:10.5204/thesis.eprints.247163
Rescuing Ischemic Brain Injury by Rewiring Mitochondrial Electron FlowPreprint
Yoval‐Sánchez, B., Guerrero, I., Chen, Q., Sosunov, S. A., Ansari, F., Siragusa, M., Konràd, C., Niatsetskaya, Z. V., Степанова, А., Starkov, A. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.19.650489
Liquid tobacco-induced optic neuropathy in the tribal population of Northeast India
Choudhury, H., Choudhury, H., Kharibam, M. D., & Choudhury, H. K. (2025) · Indian Journal of Ophthalmology · doi:10.4103/ijo.ijo_733_25
“[15] Tobacco smoke reduces mitochondrial respiration and membrane potential resulting in diminished ATP generation and enhanced oxidant content.”
The Potential for Using the Mechanism of Hypoxic Adaptation in Lower Eukaryotes
Zorov, D. B., Zorova, L. D., Babenko, V. А., Semenovich, D. S., Ivanova, A. E., Zorov, S. D., Pevzner, I. B., Plotnikov, E. Y., Silachev, D. N., & Sukhikh, G. T. (2026) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747825700527
“Hansford et al. [37] showed that in such an environment, mitochondria produce virtually no ROS, but this production increases sharply when succinate is used as a respiratory substrate for isolated mitochondria at concentrations of one millimole and above, which corresponds to the levels of…”
Métabolisme oxydatif et mitochondrial des cellules cancéreuses de prostate
Matar, C. (2011) · theses.fr (ABES) · doi:10.70675/6abb943ez119bz424fzbe51z3467241fc235
Abdellaoui, A. (2011) · theses.fr (ABES) · doi:10.70675/2be5cfefz08ebz4947z85fdz3f676fb50fe6
Andrianjafiniony, T. (2010) · theses.fr (ABES) · doi:10.70675/e8e80863z024fz49b2z87c6zd4ee4c88a3d6
Effets antitumoraux des anesthésiques locaux dans le cancer du sein
Chamaraux‐Tran, T. (2019) · theses.fr (ABES) · doi:10.70675/b5e709cfz1dc4z4f06zbce0z83159eb0e475
Delehedde, C. (2019) · theses.fr (ABES) · doi:10.70675/79b9d873z2997z43e0z95a3zddde248acdee
Développement de stratégies naturelles de cardioprotection : Quel rôle pour la mitochondries ?
Boulghobra, D. (2021) · theses.fr (ABES) · doi:10.70675/72de819azc0ebz4134zb302zc979b24377d3
Same mitochondria, different longevities : what do ants tell us about metabolic ageing ?
Kervella, M. (2023) · theses.fr (ABES) · doi:10.70675/7b57ef70z057dz4435za749zb0c6dcd534e4
Metals exposure dissociates mitochondrial NAD(P)H redox state from H₂O₂ emission
Tetteh, P. A., Kalvani, Z., Stevens, D., Sappal, R., & Kamunde, C. (2026) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2026.110639
Molecular Mechanisms of Mitochondrial Transport in Neurons
Babić, M. (2015) · UA Campus Repository (The University of Arizona)
Gan, Z. (2011) · e-Publications@Marquette (Marquette University)
Metadata
- Authors
- Hansford, R. G., Hogue, B. A., & Mildaziene, V.
- Affiliations
- National Institute on Aging (US)
- Venue
- Journal of Bioenergetics and Biomembranes
- Published
- 1997-02
- Volume
- 29
- Issue
- 1
- Pages
- 89-95
- ISSN
- 0145-479X (ISSN-L)
- 1573-6881
- OpenAlex
- W2414123687
- Cited by
- 447
- References
- 26
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 9 · 2023: 2 · 2022: 12 · 2021: 11 · 2020: 10 · 2019: 15 · 2018: 13 · 2017: 11 · 2016: 11 · 2015: 11 · 2014: 26 · 2013: 17 · 2012: 28
- FWCI
- 5.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Bioenergetics and Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Lithuanian University of Health Sciences (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- hydrogen peroxide production, heart mitochondria, mitochondrial reactive oxygen species, complex I, NAD+/NADH ratio, membrane potential, succinic acid, antimycin A, myxothiazol, manganese, superoxide dismutase, donor age, senescence, substrate specificity, inhibitor sensitivity
- MeSH terms
- Aging, Animals, Electron Transport, Hydrogen Peroxide, Mitochondria, Heart, Substrate Specificity, Succinates, Uncoupling Agents, Rats
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.