Abstract
Bacterial Multicomponent Monooxygenases (BMMs) are diiron enzymes characterized by the ability to hydroxylate a variety of hydrocarbon substrates. BMMs are naturally found in bacteria whose natural source of energy is derived from small organic compounds requiring initial hydroxylation for bacterial aerobic respiration. BMMs are of interest because the substrate transformations they perform can be useful in removing atmospheric greenhouse gases (i.e. methane) from the environment and such biocatalysts have potential applications in industrial organic syntheses. Phenol hydroxylase (PH) from Pseudomonas sp OX1 is a BMM family member essential for carrying out the oxidation of phenol to catechol but unlike the highly homologous soluble methane monoxygenase, it is unable to carry out oxidation on alkanes. Various studies suggest that the diiron coordination sphere in PH and sMMO are nearly identical, however, it is not understood how the protein scaffolds tune their reactivity toward different substrates. Here we present our efforts to explore the effects of the 2nd coordination sphere on reactivity and report on the development a screen to that would allow us search for alkane‐hydroxylating properties among a library of PH mutants.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callSimilar Papers
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
