9IQH
Crystal structure of sulfhydrylase
Summary for 9IQH
| Entry DOI | 10.2210/pdb9iqh/pdb |
| Descriptor | O-succinylhomoserine sulfhydrylase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | biosynthesis, cds quantum dots, sqr enzyme, extracellular polyphosphate, cadmium waste recycle, lyase |
| Biological source | Acidithiobacillus |
| Total number of polymer chains | 2 |
| Total formula weight | 87821.08 |
| Authors | |
| Primary citation | Li, X.J.,Wang, T.Q.,Qi, L.,Li, F.W.,Xia, Y.Z.,Zhang, C.J.,Chen, L.X.,Lin, J.Q. A one-step route for the conversion of Cd waste into CdS quantum dots by Acidithiobacillus sp. via unique biosynthesis pathways. Rsc Chem Biol, 6:281-294, 2025 Cited by PubMed Abstract: Microorganisms serve as biological factories for the synthesis of nanomaterials such as CdS quantum dots. Based on the uniqueness of sp., a one-step route was explored to directly convert cadmium waste into CdS QDs using these bacteria. First, an exhaustive study was conducted to reveal the specific pathways involved in the biosynthesis of CdS QDs. The widely known homologous enzyme, cysteine desulfhydrase, which catalyzes the synthesis of CdS QDs from a cysteine substrate, is also present in sp. and is referred to as the OSH enzyme. The structure of the OSH enzyme was determined through X-ray crystallography. Moreover, we identified two new pathways. One involved the SQR enzyme in sp., which catalyzed the formation of sulfur globules and subsequently catalyzed further reactions with GSH to release HS; subsequently, a CdS QD biosynthesis pathway was successfully constructed. The other pathway involved extracellular polyphosphate, a bacterial metabolic product, which with the addition of GSH and Cd, resulted in the formation of water-soluble fluorescent CdS QDs in the supernatant. Based on the above-described mechanism, after the bioleaching of Cd from cadmium waste by sp., CdS QDs were directly obtained from the bacterial culture supernatants. This work provides important insights into cleaner production and cadmium bioremediation with potential industrial applications. PubMed: 39802632DOI: 10.1039/d4cb00195h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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