Title
In-silico based redesign of CO-dehydrogenase catalyzing the oxidation of toxic waste CO gas for improved O2 resistance and mediator affinity
Conference Dates
September 15-19, 2019
Abstract
Carbon monoxide (CO) harmful to most creatures, is largely discharged by industrial processes in steel mill and thermal power plant. Conversion of toxic waste CO gas to safe gas or more valuable chemicals will be a great worth at this point. Interestingly, carbons and high potential electrons from CO-oxidation can be resourced as essential core parts for the chemical products by using CO-dehydrogenase (CODH) and artificial mediator. For industrial application of the enzymatic CO-oxidation, however, key issues remain that most CODHs show oxygen (O2) sensitivity and low-affinity for artificial mediator. Because steel mill waste gas such as blast furnace gas (BFG) commonly contains a little O2 and higher affinity is required to achieve higher reaction rate.
In this research, in-silico based approach was used to redesign Carboxydothermus hydrogenoformans CODH (ChCODH) II, capable of increasing O2 resistance and affinity to ethyl viologen (EV) mediator. ChCODHs belong to a group of Ni-Fe containing CODH. Among five known ChCODHs (ChCODH I-V), ChCODH II shows the highest activity toward CO but more O2 sensitive than ChCODH IV. The artificial mediator of EV functions as an electron acceptor for ChCODH II but the affinity of ChCODH II to EV mediator is known poor. As our result, more than 10 folds increase of O2 resistance was achieved for the redesigned ChCODH II enzyme, which will be definitely a working horse in the conversion of waste CO gas into value-added chemicals.
Recommended Citation
Jinhee Lee, Ho Won Hwang, Suk Min Kim, Akhtar Junaid, and Yong Hwan Kim, "In-silico based redesign of CO-dehydrogenase catalyzing the oxidation of toxic waste CO gas for improved O2 resistance and mediator affinity" in "Enzyme Engineering XXV", Huimin Zhao, University of Illinois at Urbana-Champaign, USA John Wong, Pfizer, USA Eds, ECI Symposium Series, (2019). https://dc.engconfintl.org/enzyme_xxv/61