Details
| Original language | English |
|---|---|
| Title of host publication | Methods in Enzymology |
| Publisher | Academic Press Inc. |
| Pages | 271-286 |
| Number of pages | 16 |
| Publication status | Published - 2015 |
Publication series
| Name | Methods in Enzymology |
|---|---|
| Volume | 555 |
| ISSN (Print) | 0076-6879 |
| ISSN (electronic) | 1557-7988 |
Abstract
In contrast to animals, which release the signal molecule sulfide in small amounts from cysteine and its derivates, phototrophic eukaryotes generate sulfide as an essential intermediate of the sulfur assimilation pathway. Additionally, iron-sulfur cluster turnover and cyanide detoxification might contribute to the release of sulfide in mitochondria. However, sulfide is a potent inhibitor of cytochrome c oxidase in mitochondria. Thus, efficient sulfide detoxification mechanisms are required in mitochondria to ensure adequate energy production and consequently survival of the plant cell. Two enzymes have been recently described to catalyze sulfide detoxification in mitochondria of Arabidopsis thaliana, O-acetylserine(thiol)lyase C (OAS-TL C), and the sulfur dioxygenase (SDO) ethylmalonic encephalopathy protein 1 (ETHE1). Biochemical characterization of sulfide producing and consuming enzymes in mitochondria of plants is fundamental to understand the regulatory network that enables mitochondrial sulfide homeostasis under nonstressed and stressed conditions. In this chapter, we provide established protocols to determine the activity of the sulfide releasing enzyme β-cyanoalanine synthase as well as sulfide-consuming enzymes OAS-TL and SDO. Additionally, we describe a reliable and efficient method to purify OAS-TL proteins from plant material.
Keywords
- Arabidopsis thaliana, Cytochrome c, ETHE1, Mitochondria, O-Acetylserine(thiol)lyase, oxidase, Plant, SAT affinity purification, Sulfide toxicity, Sulfur dioxygenase, β-Cyanoalanine synthase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
Cite this
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- Apa
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- BibTeX
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Methods in Enzymology. Academic Press Inc., 2015. p. 271-286 (Methods in Enzymology; Vol. 555).
Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review
}
TY - CHAP
T1 - Sulfide detoxification in plant mitochondria
AU - Birke, Hannah
AU - Hildebrandt, Tatjana M.
AU - Wirtz, Markus
AU - Hell, Rüdiger
N1 - Funding information: The authors gratefully acknowledge support of H. B. by the Landesgraduiertenförderung Baden-Württemberg, the Schmeil-Stiftung Heidelberg, and the German Research Society (grant no. He1848/13-1/14-1).
PY - 2015
Y1 - 2015
N2 - In contrast to animals, which release the signal molecule sulfide in small amounts from cysteine and its derivates, phototrophic eukaryotes generate sulfide as an essential intermediate of the sulfur assimilation pathway. Additionally, iron-sulfur cluster turnover and cyanide detoxification might contribute to the release of sulfide in mitochondria. However, sulfide is a potent inhibitor of cytochrome c oxidase in mitochondria. Thus, efficient sulfide detoxification mechanisms are required in mitochondria to ensure adequate energy production and consequently survival of the plant cell. Two enzymes have been recently described to catalyze sulfide detoxification in mitochondria of Arabidopsis thaliana, O-acetylserine(thiol)lyase C (OAS-TL C), and the sulfur dioxygenase (SDO) ethylmalonic encephalopathy protein 1 (ETHE1). Biochemical characterization of sulfide producing and consuming enzymes in mitochondria of plants is fundamental to understand the regulatory network that enables mitochondrial sulfide homeostasis under nonstressed and stressed conditions. In this chapter, we provide established protocols to determine the activity of the sulfide releasing enzyme β-cyanoalanine synthase as well as sulfide-consuming enzymes OAS-TL and SDO. Additionally, we describe a reliable and efficient method to purify OAS-TL proteins from plant material.
AB - In contrast to animals, which release the signal molecule sulfide in small amounts from cysteine and its derivates, phototrophic eukaryotes generate sulfide as an essential intermediate of the sulfur assimilation pathway. Additionally, iron-sulfur cluster turnover and cyanide detoxification might contribute to the release of sulfide in mitochondria. However, sulfide is a potent inhibitor of cytochrome c oxidase in mitochondria. Thus, efficient sulfide detoxification mechanisms are required in mitochondria to ensure adequate energy production and consequently survival of the plant cell. Two enzymes have been recently described to catalyze sulfide detoxification in mitochondria of Arabidopsis thaliana, O-acetylserine(thiol)lyase C (OAS-TL C), and the sulfur dioxygenase (SDO) ethylmalonic encephalopathy protein 1 (ETHE1). Biochemical characterization of sulfide producing and consuming enzymes in mitochondria of plants is fundamental to understand the regulatory network that enables mitochondrial sulfide homeostasis under nonstressed and stressed conditions. In this chapter, we provide established protocols to determine the activity of the sulfide releasing enzyme β-cyanoalanine synthase as well as sulfide-consuming enzymes OAS-TL and SDO. Additionally, we describe a reliable and efficient method to purify OAS-TL proteins from plant material.
KW - Arabidopsis thaliana
KW - Cytochrome c
KW - ETHE1
KW - Mitochondria
KW - O-Acetylserine(thiol)lyase
KW - oxidase
KW - Plant
KW - SAT affinity purification
KW - Sulfide toxicity
KW - Sulfur dioxygenase
KW - β-Cyanoalanine synthase
UR - http://www.scopus.com/inward/record.url?scp=84929314698&partnerID=8YFLogxK
U2 - 10.1016/bs.mie.2014.11.027
DO - 10.1016/bs.mie.2014.11.027
M3 - Contribution to book/anthology
C2 - 25747485
AN - SCOPUS:84929314698
T3 - Methods in Enzymology
SP - 271
EP - 286
BT - Methods in Enzymology
PB - Academic Press Inc.
ER -