Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain

Kimura, Yoshinobu; Toyofuku, Yukiko; Koike, Sachiko; Shibuya, Norihiro; Nagahara, Noriyuki; Lefer, David J.; Ogasawara, Yuki; Kimura, Hideo

doi:10.1038/srep14774

Cited by 192 publications

(215 citation statements)

References 40 publications

(56 reference statements)

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“…Actual reports of cellular RSS concentrations are rare, but preliminary studies provide concentrations that equal or exceed ROS (18,27). This is further supported by our calculations, above, of sulfur and oxygen turnover.…”

Section: Discussionsupporting

confidence: 79%

“…Persulfides and polysulfides can also be produced by two-electron oxidation of organic sulfur (cysteine) and transferred to a protein thiol (e.g., 3-mercaptopyruvate sulfur transferase, 3MST), forming 3MST persulfide (3MST-S-S). The hydrogen persulfide, H 2 S 3 , has recently been shown to be formed from 3MST persulfide in neuronal cells, and it may exist in micromolar concentrations (27). H 2 S can also reduce a disulfide bond (RSSR= ϩ H2S ¡ RSSH ϩ R'S).…”

Section: Discussionmentioning

confidence: 99%

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A case of mistaken identity: are reactive oxygen species actually reactive sulfide species?

DeLeon

Gao

Huang

et al. 2016

American Journal of Physiology-Regulatory, Integrative and Comp

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Stepwise one-electron reduction of oxygen to water produces reactive oxygen species (ROS) that are chemically and biochemically similar to reactive sulfide species (RSS) derived from one-electron oxidations of hydrogen sulfide to elemental sulfur. Both ROS and RSS are endogenously generated and signal via protein thiols. Given the similarities between ROS and RSS, we wondered whether extant methods for measuring the former would also detect the latter. Here, we compared ROS to RSS sensitivity of five common ROS methods: redox-sensitive green fluorescent protein (roGFP), 2', 7'-dihydrodichlorofluorescein, MitoSox Red, Amplex Red, and amperometric electrodes. All methods detected RSS and were as, or more, sensitive to RSS than to ROS. roGFP, arguably the "gold standard" for ROS measurement, was more than 200-fold more sensitive to the mixed polysulfide H2Sn(n = 1-8) than to H2O2 These findings suggest that RSS may be far more prevalent in intracellular signaling than previously appreciated and that the contribution of ROS may be overestimated. This conclusion is further supported by the observation that estimated daily sulfur metabolism and ROS production are approximately equal and the fact that both RSS and antioxidant mechanisms have been present since the origin of life, nearly 4 billion years ago, long before the rise in environmental oxygen 600 million years ago. Although ROS are assumed to be the most biologically relevant oxidants, our results question this paradigm. We also anticipate our findings will direct attention toward development of novel and clinically relevant anti-(RSS)-oxidants.

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

A case of mistaken identity: are reactive oxygen species actually reactive sulfide species?

DeLeon

Gao

Huang

et al. 2016

American Journal of Physiology-Regulatory, Integrative and Comp

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show abstract

“…Others and we have also reported that H 2 S can be mobilized from biochemical reservoirs such as acid labile sulfur (iron sulfur clusters), and sulfane sulfur (e.g. thiosulfide, protein per/polysulfide) [23], [36], [37]. Moreover, increasing evidence suggests that sulfane sulfur serves as an active form of H 2 S that is highly potent and may be responsible for some of H 2 S biological effects [18], [29].…”

Section: Introductionmentioning

confidence: 65%

Hydrogen sulfide metabolism regulates endothelial solute barrier function

et al. 2016

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Hydrogen sulfide (H2S) is an important gaseous signaling molecule in the cardiovascular system. In addition to free H2S, H2S can be oxidized to polysulfide which can be biologically active. Since the impact of H2S on endothelial solute barrier function is not known, we sought to determine whether H2S and its various metabolites affect endothelial permeability. In vitro permeability was evaluated using albumin flux and transendothelial electrical resistance. Different H2S donors were used to examine the effects of exogenous H2S. To evaluate the role of endogenous H2S, mouse aortic endothelial cells (MAECs) were isolated from wild type mice and mice lacking cystathionine γ-lyase (CSE), a predominant source of H2S in endothelial cells. In vivo permeability was evaluated using the Miles assay. We observed that polysulfide donors induced rapid albumin flux across endothelium. Comparatively, free sulfide donors increased permeability only with higher concentrations and at later time points. Increased solute permeability was associated with disruption of endothelial junction proteins claudin 5 and VE-cadherin, along with enhanced actin stress fiber formation. Importantly, sulfide donors that increase permeability elicited a preferential increase in polysulfide levels within endothelium. Similarly, CSE deficient MAECs showed enhanced solute barrier function along with reduced endogenous bound sulfane sulfur. CSE siRNA knockdown also enhanced endothelial junction structures with increased claudin 5 protein expression. In vivo, CSE genetic deficiency significantly blunted VEGF induced hyperpermeability revealing an important role of the enzyme for barrier function. In summary, endothelial solute permeability is critically regulated via exogenous and endogenous sulfide bioavailability with a prominent role of polysulfides.

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“…Sulfide and polysulfide were detected with colorimetric assays (12). Thiosulfate and sulfite were detected after monobromobimane (mBBr) derivatization by using high-pressure liquid chromatography (HPLC) (12,47). Polysulfide was produced by mixing 13 mg of sulfur power and 70 mg of sodium sulfide in 5 ml of anoxic distilled water under argon gas, as previous described (12).…”

Section: Methodsmentioning

confidence: 99%

Cytoplasmic Localization of Sulfide:Quinone Oxidoreductase and Persulfide Dioxygenase of Cupriavidus pinatubonensis JMP134

Gao

Liu

Xun

2017

Appl Environ Microbiol

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Heterotrophic bacteria have recently been reported to oxidize sulfide to sulfite and thiosulfate by using sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO). In chemolithotrophic bacteria, both SQR and PDO have been reported to function in the periplasmic space, with SQR as a peripheral membrane protein whose C terminus inserts into the cytoplasmic membrane and PDO as a soluble protein. JMP134, best known for its ability to degrade 2,4-dichlorophenoxyacetic acid and other aromatic pollutants, has a gene cluster of and encoding SQR (CpSQR) and CpPDO2. When cloned in , the enzymes are functional. Here we investigated whether they function in the periplasmic space or in the cytoplasm in heterotrophic bacteria. By using sequence analysis, biochemical detection, and green fluorescent protein (GFP)/PhoA fusion proteins, we found that CpSQR was located on the cytoplasmic side of the membrane and CpPDO2 was a soluble protein in the cytoplasm with a tendency to be peripherally located near the membrane. The location proximity of these proteins near the membrane in the cytoplasm may facilitate sulfide oxidation in heterotrophic bacteria. The information may guide the use of heterotrophic bacteria in bioremediation of organic pollutants as well as HS. Sulfide (HS, HS, and S), which is common in natural gas and wastewater, causes a serious malodor at low levels and is deadly at high levels. Microbial oxidation of sulfide is a valid bioremediation method, in which chemolithotrophic bacteria that use sulfide as the energy source are often used to remove sulfide. Heterotrophic bacteria with SQR and PDO have recently been reported to oxidize sulfide to sulfite and thiosulfate. JMP134 has been extensively characterized for its ability to degrade organic pollutants, and it also contains SQR and PDO. This paper shows the localization of SQR and PDO inside the cytoplasm in the vicinity of the membrane. The information may provide guidance for using heterotrophic bacteria in sulfide bioremediation.

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Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain

Cited by 192 publications

References 40 publications

A case of mistaken identity: are reactive oxygen species actually reactive sulfide species?

A case of mistaken identity: are reactive oxygen species actually reactive sulfide species?

Hydrogen sulfide metabolism regulates endothelial solute barrier function

Cytoplasmic Localization of Sulfide:Quinone Oxidoreductase and Persulfide Dioxygenase of Cupriavidus pinatubonensis JMP134

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