Radiolytic Modification of Sulfur-Containing Amino Acid Residues in Model Peptides:  Fundamental Studies for Protein Footprinting

2005 ◽  
Vol 77 (8) ◽  
pp. 2437-2449 ◽  
Author(s):  
Guozhong Xu ◽  
Mark R. Chance
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Protein Footprinting ◽  
Sulfur Containing ◽  
Model Peptides

Proof of delocalization-stabilization by sulfur in enolate formation during racemisation of sulfur containing amino acid residues.

1981 ◽  
Vol 22 (32) ◽  
pp. 3101-3104 ◽  
Author(s):  
M.J.O. Anteunis ◽  
F. Borremans ◽  
D. Wante ◽  
R. Schrooten
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Sulfur Containing

scholarly journals Saccharomyces cerevisiae Rhodanese RDL2 Uses the Arg Residue of the Active-Site Loop for Thiosulfate Decomposition

Antioxidants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1525
Author(s):  
Qingda Wang ◽  
Huanjie Li ◽  
Yongzhen Xia ◽  
Luying Xun ◽  
Huaiwei Liu
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Active Site ◽  
In Vitro Assays ◽  
Amino Acid Residues ◽  
Sulfane Sulfur ◽  
Sulfur Transfer ◽  
Sulfur Containing ◽  
Positively Charged

Persulfide, polysulfide and thiosulfate are examples of sulfane sulfur containing chemicals that play multiple functions in biological systems. Rhodaneses are widely present in all three kingdoms of life, which catalyze sulfur transfer among these sulfane sulfur-containing chemicals. The mechanism of how rhodaneses function is not well understood. Saccharomyces cerevisiae rhodanese 2 (RDL2) is involved in mitochondrial biogenesis and cell cycle control. Herein, we report a 2.47 Å resolution structure of RDL2 co-crystallized with thiosulfate (PDB entry: 6K6R). The presence of an extra sulfur atom Sδ, forming a persulfide bond with the Sγ atom of Cys106, was observed. Distinct from the persulfide groups in GlpE (PDB entry:1GMX) and rhobov (PDB entry:1BOI), the persulfide group of RDL2 is located in a peanut-like pocket of the neutral electrostatic field and is far away from positively charged amino acid residues of its active-site loop, suggesting no interaction between them. This finding suggests that the positively charged amino acid residues are not involved in the stabilization of the persulfide group. Activity assays indicate that the Arg111 of the active-site loop is critical for the sulfane sulfur transfer. In vitro assays indicate that Arg propels the thiosulfate decomposition. Thus, we propose that Arg can offer a hydrogen bond-rich, acidic-like microenvironment in RDL2 in which thiosulfate decomposes to release sulfane sulfur. Thr of the active-site loop of rhodaneses has the same functions as Arg. Our proposal may explain the catalyzing mechanism of rhodaneses.

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

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