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The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17
- Source :
- FEBS Letters. 503:168-172
- Publication Year :
- 2001
- Publisher :
- Wiley, 2001.
-
Abstract
- Four proteins of Paracoccus pantotrophus are required for hydrogen sulfide-, sulfur-, thiosulfate- and sulfite-dependent horse heart cytochrome c reduction. The lack of free intermediates suggested a protein-bound sulfur oxidation mechanism. The SoxY protein has a novel motif containing a cysteine residue. Electrospray ionization and matrix-assisted laser desorption ionization mass spectrometry of the SoxYZ protein revealed one mass for SoxZ and different masses for SoxY, indicating native SoxY (10 977 Da) and SoxY with additional masses of +32, +80, +112 and +144 Da, suggesting addition of sulfur, sulfite, thiosulfate and thioperoxomonosulfate. Reduction of SoxY removed the additional masses, indicating a thioether or thioester bond. N-Ethylmaleimide inhibited thiosulfate-oxidation and the kinetics suggested a turn-over-dependent mode of action. These data were evidence that the sulfur atom to be oxidized was covalently linked to the thiol moiety of the cysteine residue of SoxY and the active site of sulfur oxidation.
- Subjects :
- Spectrometry, Mass, Electrospray Ionization
Stereochemistry
Hydrogen sulfide
Electrospray ionization
Biophysics
chemistry.chemical_element
Biochemistry
S-Cysteinesulfate
Sulfur oxidation
chemistry.chemical_compound
SoxYZ protein
Bacterial Proteins
Structural Biology
Catalytic Domain
Genetics
Organic chemistry
S-Thiocysteine
Cysteine
Sulfhydryl Compounds
Molecular Biology
Thiosulfate
chemistry.chemical_classification
Paracoccus pantotrophus
biology
Active site
Paracoccus
Cell Biology
Sulfur
Molecular Weight
Kinetics
chemistry
Ethylmaleimide
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
biology.protein
Thiol
S-Thiocysteinesulfate
Oxidoreductases
Oxidation-Reduction
Protein Binding
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 503
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....b1db4b3ee20e9c0f41738cd3be4536c5