| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-129 |
Sentence |
denotes |
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis. |
| T2 |
130-252 |
Sentence |
denotes |
FeS clusters are versatile cofactors of a variety of proteins, but the mechanisms of their biosynthesis are still unknown. |
| T3 |
253-367 |
Sentence |
denotes |
The cystine C-S lyase from Synechocystis has been identified as a participant in ferredoxin FeS cluster formation. |
| T4 |
368-532 |
Sentence |
denotes |
Herein, we report on the crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8- and 1.55-A resolution, respectively. |
| T5 |
533-615 |
Sentence |
denotes |
The sulfur-containing product was unequivocally identified as cysteine persulfide. |
| T6 |
616-764 |
Sentence |
denotes |
The reactive persulfide group is fixed by a hydrogen bond to His-114 in the center of a hydrophobic pocket and is thereby shielded from the solvent. |
| T7 |
765-999 |
Sentence |
denotes |
Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly. |
