9iqh
From Proteopedia
Crystal structure of sulfhydrylase
Structural highlights
FunctionA0A2W1K030_ACIFR Catalyzes the formation of L-homocysteine from O-succinyl-L-homoserine (OSHS) and hydrogen sulfide.[HAMAP-Rule:MF_02056] Publication Abstract from PubMedMicroorganisms serve as biological factories for the synthesis of nanomaterials such as CdS quantum dots. Based on the uniqueness of Acidithiobacillus 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 Acidithiobacillus 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 Acidithiobacillus sp., which catalyzed the formation of sulfur globules and subsequently catalyzed further reactions with GSH to release H(2)S; 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(2+), resulted in the formation of water-soluble fluorescent CdS QDs in the supernatant. Based on the above-described mechanism, after the bioleaching of Cd(2+) from cadmium waste by Acidithiobacillus 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. A one-step route for the conversion of Cd waste into CdS quantum dots by Acidithiobacillus sp. via unique biosynthesis pathways.,Li XJ, Wang TQ, Qi L, Li FW, Xia YZ, Bin-Jin, Zhang CJ, Chen LX, Lin JQ RSC Chem Biol. 2024 Dec 20;6(2):281-294. doi: 10.1039/d4cb00195h. eCollection , 2025 Feb 5. PMID:39802632[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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