Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin

Taniguchi, Tadatsugu; Kimura, Tokuji

doi:10.1016/0005-2744(74)90014-x

Cited by 77 publications

(45 citation statements)

References 28 publications

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“…Using an Alexa Fluor 488-conjugated secondary antibody we were able to detect TUM1 in the cytosol and mitochondria (Fig. 8), which is consistent with the previously obtained results (15). As control, we used DAPI for visualization of the nuclei and MitoTracker DeepRed for visualization of the mitochondria.…”

Section: Indirect Immunofluorescence Of Tum1 In Hek293asupporting

confidence: 90%

“…The crystal structure of human and yeast TUM1, also in complex with 3-MP has been solved at 2.15-Å resolution (13,14). TUM1 is expressed in kidney cells, liver cells, cardiac cells, and neurological cells (15). Human individuals lacking proper formation of TUM1 were shown to excrete elevated levels of mercaptolactate-cysteine disulfide in the urine, an inborn disorder referred to as mercaptolactate-cysteine disulfiduria (16,17).…”

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confidence: 99%

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Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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Background: Localization and identification of interaction partners of two splice variants of the human 3-mercaptopyruvate sulfurtransferase TUM1. Results: We show that TUM1 interacts with proteins involved in Moco and FeS cluster biosynthesis. Conclusion: Human TUM1 is a dual localized protein in the cytosol and mitochondria with distinct roles in sulfur transfer and interaction partners. Significance: The study contributes to the sulfur transfer pathway for the biosynthesis of sulfur-containing biofactors.

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Section: Indirect Immunofluorescence Of Tum1 In Hek293asupporting

confidence: 90%

mentioning

confidence: 99%

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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“…reactions such as the formation of an ironsulphur chromophore of ferrodoxin, an important component of the respiratory chain and the overall metabolism of sulphur [9,26]. They also catalyse the direct oxidation of reduced thioredoxin by reactive oxygen species [23].…”

Section: Discussionmentioning

confidence: 99%

“…This enzyme was assayed according to the spectrophotometric method of Taniguchi and Kimura [26]. The reaction mixture contained 40 µL of Tris-HCl buffer, pH 7.4, and 15 µL mercaptopyruvate and 25 µL of KCN.…”

Section: -Mst Assaymentioning

confidence: 99%

Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds

2001

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-Cyanide detoxification is catalysed by two enzymes: rhodanese [thiosulphate: cyanide sulphurtransferase, E.C. 2.8.1.1], and 3-mercaptopyruvate sulphurtransferase [3-MST, EC. 2.8.1.2]. In the present work, the activity of the two enzymes in the crude extracts of different tissues and in the mitochondrial and cytosolic fractions of tissues from some ruminants (camels, cattle and sheep) and birds (chickens and pigeons) have been compared. Rhodanese activity was almost exclusively present in the mitochondrial fraction. In ruminants and chickens the highest activity of rhodanese was found in the liver, followed by the kidney. In pigeons, however, the enzyme activity was the highest in the kidneys. In camels' tissues, the rhodanese activity was significantly (P < 0.05) lower than in cattle or sheep, and the enzyme activities in the two latter species were similar. The activity of 3-MST in the crude extract of tissues from camels was similar to that in sheep, but higher than that in cattle. The enzyme activity was equally distributed between the mitochondrial and cytosolic fractions in the liver and kidneys of camels, cattle and sheep. Chez les ruminants et les poulets, la plus forte activité du rhodanese a été trouvée dans le foie, suivi par le rein. Cependant, chez le pigeon, l'activité enzymatique la plus forte a été détectée dans le rein. Dans les tissus du chameau, l'activité du rhodanese était significativement (P < 0,05) plus faible que chez le bovin et le mouton, et les activités enzymatiques chez ces deux dernières espèces

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“…However, maximum production was found to occur under alkaline conditions (60,62). CBS and CSE are localized to the cytoplasm, while 3MST is mainly localized to the mitochondrial matrix, with a pH of approximately 8 (45).…”

Section: Mst With Catmentioning

confidence: 99%

Hydrogen Sulfide Is a Signaling Molecule and a Cytoprotectant

Kimura

Shibuya²,

Kimura³

2012

Antioxidants & Redox Signaling

256

190

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Significance: Accumulating evidence shows that hydrogen sulfide may function as a signaling molecule in processes such as neuromodulation in the brain and smooth muscle relaxation in the vascular system. It also has a cytoprotective effect, since it can protect neurons and cardiac muscle from oxidative stress and ischemiareperfusion injury, respectively. Hydrogen sulfide can also modulate inflammation, insulin release, and angiogenesis. Recent Advances: The regulation of the activity of 3-mercaptopyruvate sulfur transferase (3MST) along with cysteine aminotransferase (CAT), one of the H 2 S producing pathways, has been demonstrated. The production of H 2 S by the pathway, which is regulated by Ca 2+ and facilitated by thioredoxin and dihydrolipoic acid, is also involved in H 2 S signaling as well as cytoprotection. Sulfur hydration of proteins by H 2 S has been proposed to modulate protein functions. H 2 S-sensitive fluorescent probes, which enable us to measure the localization of H 2 S in real time, have been developed. Critical Issues: The basal concentrations of H 2 S have recently been measured and found to be much lower than those initially reported. However, the concentration of H 2 S reached in stimulated cells, as well as the regulation of H 2 S producing enzymes is not well understood. It has been proposed that some of the effects of H 2 S on the regulation of enzymes and receptors might be explained through the properties of sulfane sulfur (S 0 ), another form of active sulfur. Future Directions: The determination of H 2 S concentrations in activated cells using new methods including H 2 S-sensitive fluorescent probes, as well as the investigation of the effects of H 2 S using specific inhibitors, may provide better understanding of the physiological function of this molecule. Clarifying mechanisms of H 2 S activity may also facilitate the development of new therapeutic compounds. Antioxid. Redox Signal. 17, 45-57.

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Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin

Cited by 77 publications

References 28 publications

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds

Hydrogen Sulfide Is a Signaling Molecule and a Cytoprotectant

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