한빛사 논문
Suk Min Kim 1,4, Jinhee Lee1,4, Sung Heuck Kang 1,2,4, Yoonyoung Heo 3,4, Hye-Jin Yoon3, Ji-Sook Hahn2, Hyung Ho Lee 3,5,* and Yong Hwan Kim 1,5,*
1School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, Republic of Korea. 2School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea. 3Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, Republic of Korea. 4These authors contributed equally: Suk Min Kim, Jinhee Lee, Sung Heuck Kang, Yoonyoung Heo. 5These authors jointly supervised this work: Hyung Ho Lee, Yong Hwan Kim.
*Corresponding author.
Abstract
Ni–Fe carbon monoxide dehydrogenases (CODHs) are nearly diffusion-limited biocatalysts that oxidize CO. Their O2 sensitivity, however, is a major drawback for industrial applications. Here we compare the structures of a fast CODH with a high O2 sensitivity (ChCODH-II) and a slower CODH with a lower O2 sensitivity (ChCODH-IV) (Ch, Carboxydothermus hydrogenoformans). Some variants obtained by simple point mutations of the bottleneck residue (A559) in the gas tunnel showed 61–148-fold decreases in O2 sensitivity while maintaining high turnover rates. The variant structure A559W showed obstruction of one gas tunnel, and molecular dynamics supported the locked position of the mutated side chain in the tunnel. The variant was exposed to different gas mixtures, from simple synthetic gas to sophisticated real flue from a steel mill. Its catalytic properties remained unchanged, even at high O2 levels, and the efficiency was maintained for multiple cycles of CO detoxification/regeneration.
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