In:
Applied and Environmental Microbiology, American Society for Microbiology, Vol. 88, No. 3 ( 2022-02-08)
Abstract:
Sulfur-oxidizing bacteria can oxidize hydrogen sulfide (H 2 S) to produce sulfur globules. Although the process is common, the pathway is unclear. In recombinant Escherichia coli and wild-type Corynebacterium vitaeruminis DSM 20294 with sulfide:quinone oxidoreductase (SQR) but no enzymes to oxidize zero valence sulfur, SQR oxidized H 2 S into short-chain inorganic polysulfide (H 2 S n , n ≥ 2) and organic polysulfide (RS n H, n ≥ 2), which reacted with each other to form long-chain GS n H ( n ≥ 2) and H 2 S n before producing octasulfur (S 8 ), the main component of elemental sulfur. GS n H also reacted with glutathione (GSH) to form GS n G ( n ≥ 2) and H 2 S; H 2 S was again oxidized by SQR. After GSH was depleted, SQR simply oxidized H 2 S to H 2 S n , which spontaneously generated S 8 . S 8 aggregated into sulfur globules in the cytoplasm. The results highlight the process of sulfide oxidation to S 8 globules in the bacterial cytoplasm and demonstrate the potential of using heterotrophic bacteria with SQR to convert toxic H 2 S into relatively benign S 8 globules. IMPORTANCE Our results provide evidence of H 2 S oxidation producing octasulfur globules via sulfide:quinone oxidoreductase (SQR) catalysis and spontaneous reactions in the bacterial cytoplasm. Since the process is an important event in geochemical cycling, a better understanding facilitates further studies and provides theoretical support for using heterotrophic bacteria with SQR to oxidize toxic H 2 S into sulfur globules for recovery.
Type of Medium:
Online Resource
ISSN:
0099-2240
,
1098-5336
DOI:
10.1128/aem.01941-21
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
2022
detail.hit.zdb_id:
223011-2
detail.hit.zdb_id:
1478346-0
SSG:
12
