TY - JOUR
T1 - Sulfur Redox Cycling Dependent Abiotic Ferrihydrite Reduction by a Desulfitobacterium hafniense
AU - Li, Guo Xiang
AU - Chen, Xue Ping
AU - Wang, Xin Nan
AU - Chen, Zheng
AU - Bao, Peng
N1 - Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/5/17
Y1 - 2018/5/17
N2 - Biogeochemical interactions of iron and sulfur drive their cycles in many environments, which makes understanding the mechanism of sulfur redox cycling dependent abiotic iron(III) reduction by sulfate-reducing bacteria (SRB) particularly important. Here, we present a newly isolated Desulfitobacterium hafniense strain DH with the potential of reducing sulfate, sulfite, thiosulfate, and elemental sulfur from a paddy soil. Strain DH cannot enzymatically reduce ferrihydrite, but it can abiotically reduce ferrihydrite through extracellular electron transfer with biogenic sulfide or other sulfur compounds acting as electron shuttles. Sulfite, elemental sulfur, and thiosulfate, the oxidation products of sulfide, complete the sulfur cycle between ferrihydrite and strain DH. The presence of strain DH at the ferrihydrite surface results in mineral dissolution and secondary mineralization. Proteomic analysis revealed that the expression level of sulfur reduction functional protein DsrC and a thiosulfate reductase in the sulfide/ferrihydrite amendment group was 1.79 and 1.99 times higher, respectively, than in the sulfide-only amendment setup. On the other hand, the protein expression level of DsrAB showed no significant variation. A number of carbon metabolism enzymes, including succinate dehydrogenase (2.46 fold), fumarate reductase (2.64 fold), acetyl-coenzyme A synthetase (2.64 fold) and phosphoenolpyruvate synthase (3.4 fold), were up-regulated significantly due to the stimulation of released ferrous ion that was generated during the sulfur redox cycling dependent abiotic ferrihydrite reduction process. This result confirms the important role of DsrC and thiosulfate reductase in sulfur redox cycling dependent abiotic ferrihydrite reduction. Sulfur redox cycling dependent abiotic iron oxide reduction mediated by SRB might be a widespread process in the environment.
AB - Biogeochemical interactions of iron and sulfur drive their cycles in many environments, which makes understanding the mechanism of sulfur redox cycling dependent abiotic iron(III) reduction by sulfate-reducing bacteria (SRB) particularly important. Here, we present a newly isolated Desulfitobacterium hafniense strain DH with the potential of reducing sulfate, sulfite, thiosulfate, and elemental sulfur from a paddy soil. Strain DH cannot enzymatically reduce ferrihydrite, but it can abiotically reduce ferrihydrite through extracellular electron transfer with biogenic sulfide or other sulfur compounds acting as electron shuttles. Sulfite, elemental sulfur, and thiosulfate, the oxidation products of sulfide, complete the sulfur cycle between ferrihydrite and strain DH. The presence of strain DH at the ferrihydrite surface results in mineral dissolution and secondary mineralization. Proteomic analysis revealed that the expression level of sulfur reduction functional protein DsrC and a thiosulfate reductase in the sulfide/ferrihydrite amendment group was 1.79 and 1.99 times higher, respectively, than in the sulfide-only amendment setup. On the other hand, the protein expression level of DsrAB showed no significant variation. A number of carbon metabolism enzymes, including succinate dehydrogenase (2.46 fold), fumarate reductase (2.64 fold), acetyl-coenzyme A synthetase (2.64 fold) and phosphoenolpyruvate synthase (3.4 fold), were up-regulated significantly due to the stimulation of released ferrous ion that was generated during the sulfur redox cycling dependent abiotic ferrihydrite reduction process. This result confirms the important role of DsrC and thiosulfate reductase in sulfur redox cycling dependent abiotic ferrihydrite reduction. Sulfur redox cycling dependent abiotic iron oxide reduction mediated by SRB might be a widespread process in the environment.
KW - Abiotic reduction
KW - DsrAB
KW - DsrC
KW - Extracellular electron transfer
KW - Mineralization
KW - Thiosulfate reductase
UR - http://www.scopus.com/inward/record.url?scp=85047180942&partnerID=8YFLogxK
U2 - 10.1021/acsearthspacechem.8b00012
DO - 10.1021/acsearthspacechem.8b00012
M3 - Article
AN - SCOPUS:85047180942
SN - 2472-3452
VL - 2
SP - 496
EP - 505
JO - ACS Earth and Space Chemistry
JF - ACS Earth and Space Chemistry
IS - 5
ER -