Abstract:
:2(S)-dihydroxypropanesulfonate (DHPS) is a microbial degradation product of 6-deoxy-6-sulfo-d-glucopyranose (sulfoquinovose), a component of plant sulfolipid with an estimated annual production of 1010 tons. DHPS is also at millimolar levels in highly abundant marine phytoplankton. Its degradation and sulfur recycling by microbes, thus, play important roles in the biogeochemical sulfur cycle. However, DHPS degradative pathways in the anaerobic biosphere are not well understood. Here, we report the discovery and characterization of two O2-sensitive glycyl radical enzymes that use distinct mechanisms for DHPS degradation. DHPS-sulfolyase (HpsG) in sulfate- and sulfite-reducing bacteria catalyzes C-S cleavage to release sulfite for use as a terminal electron acceptor in respiration, producing H2S. DHPS-dehydratase (HpfG), in fermenting bacteria, catalyzes C-O cleavage to generate 3-sulfopropionaldehyde, subsequently reduced by the NADH-dependent sulfopropionaldehyde reductase (HpfD). Both enzymes are present in bacteria from diverse environments including human gut, suggesting the contribution of enzymatic radical chemistry to sulfur flux in various anaerobic niches.
journal_name
Proc Natl Acad Sci U S Aauthors
Liu J,Wei Y,Lin L,Teng L,Yin J,Lu Q,Chen J,Zheng Y,Li Y,Xu R,Zhai W,Liu Y,Liu Y,Cao P,Ang EL,Zhao H,Yuchi Z,Zhang Ydoi
10.1073/pnas.2003434117subject
Has Abstractpub_date
2020-07-07 00:00:00pages
15599-15608issue
27eissn
0027-8424issn
1091-6490pii
2003434117journal_volume
117pub_type
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