TY - JOUR
T1 - A novel soluble di-iron monooxygenase from the soil bacterium Solimonas soli
AU - Yang, Sui Nin Nicholas
AU - Haritos, Victoria
AU - Kertesz, Michael A.
AU - Coleman, Nicholas V.
N1 - Funding Information:
We thank Professor Che Ok Jeon (Chung‐Ang University) for kindly providing the culture of DCY‐12. This research was supported by internal funding from the University of Sydney. Open access publishing facilitated by Macquarie University, as part of the Wiley ‐ Macquarie University agreement via the Council of Australian University Librarians. S. soli
Publisher Copyright:
© 2024 The Authors. Environmental Microbiology published by Applied Microbiology International and John Wiley & Sons Ltd.
PY - 2024/2
Y1 - 2024/2
N2 - Soluble di-iron monooxygenase (SDIMO) enzymes enable insertion of oxygen into diverse substrates and play significant roles in biogeochemistry, bioremediation and biocatalysis. An unusual SDIMO was detected in an earlier study in the genome of the soil organism Solimonas soli, but was not characterized. Here, we show that the S. soli SDIMO is part of a new clade, which we define as ‘Group 7’; these share a conserved gene organization with alkene monooxygenases but have only low amino acid identity. The S. soli genes (named zmoABCD) could be functionally expressed in Pseudomonas putida KT2440 but not in Escherichia coli TOP10. The recombinants made epoxides from C2-C8 alkenes, preferring small linear alkenes (e.g. propene), but also epoxidating branched, carboxylated and chlorinated substrates. Enzymatic epoxidation of acrylic acid was observed for the first time. ZmoABCD oxidised the organochlorine pollutants vinyl chloride (VC) and cis-1,2-dichloroethene (cDCE), with the release of inorganic chloride from VC but not cDCE. The original host bacterium S. soli could not grow on any alkenes tested but grew well on phenol and n-octane. Further work is needed to link ZmoABCD and the other Group 7 SDIMOs to specific physiological and ecological roles.
AB - Soluble di-iron monooxygenase (SDIMO) enzymes enable insertion of oxygen into diverse substrates and play significant roles in biogeochemistry, bioremediation and biocatalysis. An unusual SDIMO was detected in an earlier study in the genome of the soil organism Solimonas soli, but was not characterized. Here, we show that the S. soli SDIMO is part of a new clade, which we define as ‘Group 7’; these share a conserved gene organization with alkene monooxygenases but have only low amino acid identity. The S. soli genes (named zmoABCD) could be functionally expressed in Pseudomonas putida KT2440 but not in Escherichia coli TOP10. The recombinants made epoxides from C2-C8 alkenes, preferring small linear alkenes (e.g. propene), but also epoxidating branched, carboxylated and chlorinated substrates. Enzymatic epoxidation of acrylic acid was observed for the first time. ZmoABCD oxidised the organochlorine pollutants vinyl chloride (VC) and cis-1,2-dichloroethene (cDCE), with the release of inorganic chloride from VC but not cDCE. The original host bacterium S. soli could not grow on any alkenes tested but grew well on phenol and n-octane. Further work is needed to link ZmoABCD and the other Group 7 SDIMOs to specific physiological and ecological roles.
UR - http://www.scopus.com/inward/record.url?scp=85182442547&partnerID=8YFLogxK
U2 - 10.1111/1462-2920.16567
DO - 10.1111/1462-2920.16567
M3 - Article
C2 - 38233213
AN - SCOPUS:85182442547
SN - 1462-2912
VL - 26
JO - Environmental Microbiology
JF - Environmental Microbiology
IS - 2
M1 - e16567
ER -