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Term	Abbreviation	Description
Succinate dehydrogenase	SDH	Succinate dehydrogenase is a TCA cycle enzyme converting succinate to fumarate while reducing FAD to FADH₂. SDH is the largest component of the mt-inner membrane Complex II (CII) and thus part of the TCA cycle and electron transfer pathway.
Succinate transport		The dicarboxylate carrier catalyses the electroneutral exchange of succinate^2- for HPO_4-^2-.
Succinyl-CoA ligase	SUCLA, SUCLG	Succinyl-CoA ligase (SUCLA or SUCLG) is a TCA cycle enzyme converting succinyl-CoA + ADP or (GDP) + Pi to succinate + ATP (GTP). Two different isoforms exsist: SUCLA (EC: 6.2.1.5) is the ATP-forming isoenzyme, SUCLG (EC: 6.2.1.4) is the GTP-forming isoenzyme. Both reactions are reversible. This reaction is attributed to mitochondrial substrate-level phosphorylation, which is considered as an alternative way of ATP synthesis because it is partially independent from the respiratory chain and from the mitochondrial proton motive force.
Sulfide quinone reductase	SQR	Sulfide quinone reductase (SQR) is involved in electron transfer from sulfide which is used as a hydrogen donor by the mitochondrial respiratory system. SQR is associated with a dioxygenase and a sulfur transferase to release thiosulfate (H₂S₂O₃).
Sulfite oxidase	SO	Sulfite oxidase (SO) is a dimeric enzyme, located in the intermembrane space of mitochondria, with each monomer containing a single Mo cofactor and cyt b5-type heme [1]. SO catalyzes the oxidation of sulfite to sulfate as the terminal step in the metabolism of sulfur amino acids and is vital for human health. Inherited mutations in SO result in severe neurological problems, stunted brain growth, and early death [2]. Function: SO catalyzes the terminal reaction in the oxidative degradation of sulfur amino acids with the formation of a sulfate, electrons pass to cytochrom c and are further utilized in the respiratory system. Sulfite + O₂ + H₂O --> Sulfate + H₂O₂ Localization: The level of expression of SO differs in various tissues with main predominant localization in liver, kidney, skeletal muscle, heart, placenta, and brain in humans and liver, kidney, heart, brain, and lung in rats [3]. Deficiency: SO is vital for metabolic pathways of sulfur amino acids (cysteine and methionine). Complete lack of this enzyme, typically caused by gene mutation, leads to lethal disease called sulfite oxidase deficiency characterized by neurological abnormalities with brain atrophy.
Superoxide dismutase	SOD	Mammalian superoxide dismutase (SOD) exists in three forms, of which the Mn-SOD occurs in mitochondria (mtSOD, SOD2; 93 kD homotetramer) and many bacteria, in contrast to the Cu-Zn forms of SOD (cytosolic SOD1, extracellular SOD3 anchored to the extracellular matrix and cell surface). Superoxide anion (O₂^•-) is a major reactive oxygen species (ROS) which is dismutated by SOD to oxygen and H₂O₂.
Thioredoxin reductase	TrxR	Thioredoxin reductase (TrxR) is a family of enzymes able to reduce thioredoxin in mammals.
Tricarboxylate carrier		The tricarboxylate carrier in the inner mt-membrane exchanges malate^2- for citrate^3- or isocitrate^3-, with co-transport of H⁺.

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