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Article ; Online: A critical assessment of the role of creatine in brown adipose tissue thermogenesis.

Nicholls, David G / Brand, Martin D

Nature metabolism

2023 Volume 5, Issue 1, Page(s) 21–28

Abstract: Brown adipose tissue is specialized for non-shivering thermogenesis, combining lipolysis with an extremely active mitochondrial electron transport chain and a unique regulated uncoupling protein, UCP1, allowing unrestricted respiration. Current ... ...

Abstract	Brown adipose tissue is specialized for non-shivering thermogenesis, combining lipolysis with an extremely active mitochondrial electron transport chain and a unique regulated uncoupling protein, UCP1, allowing unrestricted respiration. Current excitement focuses on the presence of brown adipose tissue in humans and the possibility that it may contribute to diet-induced thermogenesis, countering obesity and obesity-related disease as well as protecting cardio-metabolic health. In common with other tissues displaying a high, variable respiration, the tissue possesses a creatine pool and mitochondrial and cytosolic creatine kinase isoforms. Genetic and pharmacological manipulation of these components have pleiotropic effects that appear to influence diet- and cold-induced metabolism in vivo and modeled in vitro. These findings have been used to advance the concept of a UCP1-independent diet-induced thermogenic mechanism based on a dissipative hydrolysis of phosphocreatine in beige and brown adipose tissue. Here we review the in vivo and in vitro experimental basis for this hypothesis, and explore alternative explanations. We conclude that there is currently no convincing evidence for a significant futile creatine cycle in these tissues.
MeSH term(s)	Humans ; Adipose Tissue, Brown/metabolism ; Creatine/metabolism ; Obesity/metabolism ; Diet ; Thermogenesis
Chemical Substances	Creatine (MU72812GK0)
Language	English
Publishing date	2023-01-09
Publishing country	Germany
Document type	Journal Article ; Review
ISSN	2522-5812
ISSN (online)	2522-5812
DOI	10.1038/s42255-022-00718-2
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Article ; Online: Riding the tiger - physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix.

Brand, Martin D

Critical reviews in biochemistry and molecular biology

2020 Volume 55, Issue 6, Page(s) 592–661

Abstract: Elevated mitochondrial matrix superoxide and/or hydrogen peroxide concentrations drive a wide range of physiological responses and pathologies. Concentrations of superoxide and hydrogen peroxide in the mitochondrial matrix are set mainly by rates of ... ...

Abstract	Elevated mitochondrial matrix superoxide and/or hydrogen peroxide concentrations drive a wide range of physiological responses and pathologies. Concentrations of superoxide and hydrogen peroxide in the mitochondrial matrix are set mainly by rates of production, the activities of superoxide dismutase-2 (SOD2) and peroxiredoxin-3 (PRDX3), and by diffusion of hydrogen peroxide to the cytosol. These considerations can be used to generate criteria for assessing whether changes in matrix superoxide or hydrogen peroxide are both necessary and sufficient to drive redox signaling and pathology: is a phenotype affected by suppressing superoxide and hydrogen peroxide production; by manipulating the levels of SOD2, PRDX3 or mitochondria-targeted catalase; and by adding mitochondria-targeted SOD/catalase mimetics or mitochondria-targeted antioxidants? Is the pathology associated with variants in SOD2 and PRDX3 genes? Filtering the large literature on mitochondrial redox signaling using these criteria highlights considerable evidence that mitochondrial superoxide and hydrogen peroxide drive physiological responses involved in cellular stress management, including apoptosis, autophagy, propagation of endoplasmic reticulum stress, cellular senescence, HIF1α signaling, and immune responses. They also affect cell proliferation, migration, differentiation, and the cell cycle. Filtering the huge literature on pathologies highlights strong experimental evidence that 30-40 pathologies may be driven by mitochondrial matrix superoxide or hydrogen peroxide. These can be grouped into overlapping and interacting categories: metabolic, cardiovascular, inflammatory, and neurological diseases; cancer; ischemia/reperfusion injury; aging and its diseases; external insults, and genetic diseases. Understanding the involvement of mitochondrial matrix superoxide and hydrogen peroxide concentrations in these diseases can facilitate the rational development of appropriate therapies.
MeSH term(s)	Animals ; Antioxidants/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Mitochondria/metabolism ; Oxidation-Reduction ; Reactive Oxygen Species/metabolism ; Superoxides/metabolism ; Thioredoxins/metabolism
Chemical Substances	Antioxidants ; Reactive Oxygen Species ; Superoxides (11062-77-4) ; Thioredoxins (52500-60-4) ; Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2020-11-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1000977-2
ISSN	1549-7798 ; 1381-3455 ; 1040-9238
ISSN (online)	1549-7798
ISSN	1381-3455 ; 1040-9238
DOI	10.1080/10409238.2020.1828258
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Article ; Online: Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling.

Brand, Martin D

Free radical biology & medicine

2016 Volume 100, Page(s) 14–31

Abstract: This review examines the generation of reactive oxygen species by mammalian mitochondria, and the status of different sites of production in redox signaling and pathology. Eleven distinct mitochondrial sites associated with substrate oxidation and ... ...

Abstract	This review examines the generation of reactive oxygen species by mammalian mitochondria, and the status of different sites of production in redox signaling and pathology. Eleven distinct mitochondrial sites associated with substrate oxidation and oxidative phosphorylation leak electrons to oxygen to produce superoxide or hydrogen peroxide: oxoacid dehydrogenase complexes that feed electrons to NAD
Language	English
Publishing date	2016-11
Publishing country	United States
Document type	Review ; Journal Article
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2016.04.001
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Zs.A 2109: Show issues

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Article ; Online: Effects of sugars, fatty acids and amino acids on cytosolic and mitochondrial hydrogen peroxide release from liver cells.

Fang, Jingqi / Zhang, Yini / Gerencser, Akos A / Brand, Martin D

Free radical biology & medicine

2022 Volume 188, Page(s) 92–102

Abstract: The rates of formation of superoxide and hydrogen peroxide at different electron-donating sites in isolated mitochondria are critically dependent on the substrates that are added, through their effects on the reduction level of each site and the ... ...

Abstract	The rates of formation of superoxide and hydrogen peroxide at different electron-donating sites in isolated mitochondria are critically dependent on the substrates that are added, through their effects on the reduction level of each site and the components of the protonmotive force. However, in intact cells the acute effects of added substrates on different sites of cytosolic and mitochondrial hydrogen peroxide production are unclear. Here we tested the effects of substrate addition on cytosolic and mitochondrial hydrogen peroxide release from intact AML12 liver cells. In 30-min starved cells replete with endogenous substrates, addition of glucose, fructose, palmitate, alanine, leucine or glutamine had no effect on the rate or origin of cellular hydrogen peroxide release. However, following 150-min starvation of the cells to deplete endogenous glycogen (and other substrates), cellular hydrogen peroxide production, particularly from NADPH oxidases (NOXs), was decreased, GSH/GSSH ratio increased, and antioxidant gene expression was unchanged. Addition of glucose or glutamine (but not the other substrates) increased hydrogen peroxide release. There were similar relative increases from each of the three major sites of production: mitochondrial sites I
MeSH term(s)	Adenosine Triphosphate/metabolism ; Amino Acids/metabolism ; Fatty Acids/metabolism ; Glucose/metabolism ; Glutamine/metabolism ; Hydrogen Peroxide/metabolism ; Liver/metabolism ; Mitochondria/metabolism ; NAD/metabolism ; NADPH Oxidases/metabolism ; Sugars/metabolism ; Sugars/pharmacology ; Superoxides/metabolism
Chemical Substances	Amino Acids ; Fatty Acids ; Sugars ; Glutamine (0RH81L854J) ; NAD (0U46U6E8UK) ; Superoxides (11062-77-4) ; Adenosine Triphosphate (8L70Q75FXE) ; Hydrogen Peroxide (BBX060AN9V) ; NADPH Oxidases (EC 1.6.3.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2022-06-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2022.06.225
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Article: The role of mitochondria in longevity and healthspan.

Brand, Martin D

Longevity & healthspan

2014 Volume 3, Page(s) 7

Abstract: The role of mitochondria in aging and disease remains contentious more than 40 years after the mitochondrial free radical theory of aging was first proposed. As part of a wider cross-journal series on contemporary mitochondrial biology, Longevity & ... ...

Abstract	The role of mitochondria in aging and disease remains contentious more than 40 years after the mitochondrial free radical theory of aging was first proposed. As part of a wider cross-journal series on contemporary mitochondrial biology, Longevity & Healthspan presents a thematic series of four reviews that discuss the evidence for and against the modern incarnations of the theory, and examine the relevance of mitochondrial membrane phospholipid unsaturation and the interactions of mitochondria with sex hormones.
Language	English
Publishing date	2014-05-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2682223-4
ISSN	2046-2395
ISSN	2046-2395
DOI	10.1186/2046-2395-3-7
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Article ; Online: Production of superoxide and hydrogen peroxide in the mitochondrial matrix is dominated by site I

Fang, Jingqi / Wong, Hoi-Shan / Brand, Martin D

Redox biology

2020 Volume 37, Page(s) 101722

Abstract: Understanding how mitochondria contribute to cellular oxidative stress and drive signaling and disease is critical, but quantitative assessment is difficult. Our previous studies of cultured C2C12 cells used inhibitors of specific sites of superoxide and ...

Abstract	Understanding how mitochondria contribute to cellular oxidative stress and drive signaling and disease is critical, but quantitative assessment is difficult. Our previous studies of cultured C2C12 cells used inhibitors of specific sites of superoxide and hydrogen peroxide production to show that mitochondria generate about half of the hydrogen peroxide released by the cells, and site I
MeSH term(s)	Animals ; Cell Line ; Electron Transport Complex I/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Mice ; Mitochondria/metabolism ; Rats ; Superoxides/metabolism
Chemical Substances	Superoxides (11062-77-4) ; Hydrogen Peroxide (BBX060AN9V) ; Electron Transport Complex I (EC 7.1.1.2)
Language	English
Publishing date	2020-09-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2020.101722
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Article ; Online: Controlled power: how biology manages succinate-driven energy release.

Mookerjee, Shona A / Gerencser, Akos A / Watson, Mark A / Brand, Martin D

Biochemical Society transactions

2021 Volume 49, Issue 6, Page(s) 2929–2939

Abstract: Oxidation of succinate by mitochondria can generate a higher protonmotive force (pmf) than can oxidation of NADH-linked substrates. Fundamentally, this is because of differences in redox potentials and gearing. Biology adds kinetic constraints that tune ... ...

Abstract	Oxidation of succinate by mitochondria can generate a higher protonmotive force (pmf) than can oxidation of NADH-linked substrates. Fundamentally, this is because of differences in redox potentials and gearing. Biology adds kinetic constraints that tune the oxidation of NADH and succinate to ensure that the resulting mitochondrial pmf is suitable for meeting cellular needs without triggering pathology. Tuning within an optimal range is used, for example, to shift ATP consumption between different consumers. Conditions that overcome these constraints and allow succinate oxidation to drive pmf too high can cause pathological generation of reactive oxygen species. We discuss the thermodynamic properties that allow succinate oxidation to drive pmf higher than NADH oxidation, and discuss the evidence for kinetic tuning of ATP production and for pathologies resulting from substantial succinate oxidation in vivo.
MeSH term(s)	Animals ; Energy Metabolism ; Mitochondria/metabolism ; Succinic Acid/metabolism ; Thermodynamics
Chemical Substances	Succinic Acid (AB6MNQ6J6L)
Language	English
Publishing date	2021-12-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20211032
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Zs.A 944: Show issues

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Article ; Online: Generation of superoxide and hydrogen peroxide by side reactions of mitochondrial 2-oxoacid dehydrogenase complexes in isolation and in cells.

Bunik, Victoria I / Brand, Martin D

Biological chemistry

2018 Volume 399, Issue 5, Page(s) 407–420

Abstract: Mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or ... ...

Abstract	Mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or hydrogen peroxide in defined reactions by leaking electrons to oxygen. Studies using isolated mitochondria in media mimicking cytosol suggest that the 2-oxoacid dehydrogenase complexes contribute little to the production of superoxide or hydrogen peroxide relative to other mitochondrial sites at physiological steady states. However, the contributions may increase under pathological conditions, in accordance with the high maximum capacities of superoxide or hydrogen peroxide-generating reactions of the complexes, established in isolated mitochondria. We assess available data on the use of modulations of enzyme activity to infer superoxide or hydrogen peroxide production from particular 2-oxoacid dehydrogenase complexes in cells, and limitations of such methods to discriminate specific superoxide or hydrogen peroxide sources in vivo.
MeSH term(s)	3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/chemistry ; 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/metabolism ; Animals ; Humans ; Hydrogen Peroxide/metabolism ; Molecular Structure ; Reactive Oxygen Species/metabolism ; Superoxides/metabolism
Chemical Substances	Reactive Oxygen Species ; Superoxides (11062-77-4) ; Hydrogen Peroxide (BBX060AN9V) ; 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) (EC 1.2.4.4)
Language	English
Publishing date	2018-01-12
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2017-0284
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Article ; Online: Site IQ in mitochondrial complex I generates S1QEL-sensitive superoxide/hydrogen peroxide in both the reverse and forward reactions.

Gibbs, Edwin T / Lerner, Chad A / Watson, Mark A / Wong, Hoi-Shan / Gerencser, Akos A / Brand, Martin D

The Biochemical journal

2023 Volume 480, Issue 5, Page(s) 363–384

Abstract: Superoxide/hydrogen peroxide production by site IQ in complex I of the electron transport chain is conventionally assayed during reverse electron transport (RET) from ubiquinol to NAD. However, S1QELs (specific suppressors of superoxide/hydrogen peroxide ...

Abstract	Superoxide/hydrogen peroxide production by site IQ in complex I of the electron transport chain is conventionally assayed during reverse electron transport (RET) from ubiquinol to NAD. However, S1QELs (specific suppressors of superoxide/hydrogen peroxide production by site IQ) have potent effects in cells and in vivo during presumed forward electron transport (FET). Therefore, we tested whether site IQ generates S1QEL-sensitive superoxide/hydrogen peroxide during FET (site IQf), or alternatively, whether RET and associated S1QEL-sensitive superoxide/hydrogen peroxide production (site IQr) occurs in cells under normal conditions. We introduce an assay to determine if electron flow through complex I is thermodynamically forward or reverse: on blocking electron flow through complex I, the endogenous matrix NAD pool will become more reduced if flow before the challenge was forward, but more oxidised if flow was reverse. Using this assay we show in the model system of isolated rat skeletal muscle mitochondria that superoxide/hydrogen peroxide production by site IQ can be equally great whether RET or FET is running. We show that sites IQr and IQf are equally sensitive to S1QELs, and to rotenone and piericidin A, inhibitors that block the Q-site of complex I. We exclude the possibility that some sub-fraction of the mitochondrial population running site IQr during FET is responsible for S1QEL-sensitive superoxide/hydrogen peroxide production by site IQ. Finally, we show that superoxide/hydrogen peroxide production by site IQ in cells occurs during FET, and is S1QEL-sensitive.
MeSH term(s)	Rats ; Animals ; Superoxides/metabolism ; Hydrogen Peroxide/metabolism ; NAD/metabolism ; Mitochondria/metabolism ; Electron Transport ; Electron Transport Complex I/metabolism ; Electron Transport Complex I/pharmacology
Chemical Substances	Superoxides (11062-77-4) ; Hydrogen Peroxide (BBX060AN9V) ; NAD (0U46U6E8UK) ; Electron Transport Complex I (EC 7.1.1.2)
Language	English
Publishing date	2023-03-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20220611
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Article ; Online: The Whys and Hows of Calculating Total Cellular ATP Production Rate.

Handel, Megan E / Brand, Martin D / Mookerjee, Shona A

Trends in endocrinology and metabolism: TEM

2019 Volume 30, Issue 7, Page(s) 412–416

Abstract: Quantifying total cellular ATP production rate has become easier with recent technology and is essential to understanding energy metabolism in cells and tissues. We review fundamental concepts for determining total cellular ATP production rate from ... ...

Abstract	Quantifying total cellular ATP production rate has become easier with recent technology and is essential to understanding energy metabolism in cells and tissues. We review fundamental concepts for determining total cellular ATP production rate from measurements of oxygen consumption and acidification rates and discuss their application to answering biological questions.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Cell Differentiation/genetics ; Cell Differentiation/physiology ; Energy Metabolism/genetics ; Energy Metabolism/physiology ; Humans ; Oxygen Consumption/genetics ; Oxygen Consumption/physiology
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2019-05-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/j.tem.2019.04.007
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