120th General Meeting of the KCS

Type Poster Presentation
Area Life Chemistry
Room No. Exhibition Hall 2+3
Time 10월 19일 (목요일) 11:00~12:30
Code BIO.P-251
Subject Component interactions between hydroxylase and auxiliary enzymes from Methylosinus sporium strain 5
Authors Seung Jae Lee*, Min Young Song
Department of Chemistry, Chonbuk National University, Korea
Abstract The studies of sMMO have focused on Methylococcus capsulatus Bath (M. capsulatus) and Methylosinus trichosporium OB3b (M. trichoporium) for last 25 years, but mechanistic studies are still needed in order to understand methane conversion to methanol. Enzymatic mechanisms and chemical interactions of sMMO which belong to bacterial multicomponent (BMM) systems are required to understand. To date, findings are retarded due to the difficulties of complex formation during enzymatic studies. This implies that MMOB and MMOR controls the oxidation reactions of hydroxylase. These studies will address those questions to develop new enzymes for the production of methanol from methane gas. The structure and function of the active site (di-iron) will be studied using rapid freeze quench (RFQ) spectroscopic methods. The activation energy to break the C-H bond in methane is significantly high (104.9 kcal/mol). Therefore, intermediate structures during enzyme catalysis need to be elucidated when bound to substrate during the catalytic cycle. In addition, electron transfer mechanisms will be performed to get catalytic activities. X-ray crystallography of MMOH-MMOR will provide insight into electron transfer pathways. Structural and functional consequences from basic studies will be applied in E. coli or other natural bacterial systems for practical use. MMOB and MMOR interactions with engineered enzymes will accelerate the oxidation of specific substrates. The chaperon proteins will be modified to enhance performance in heterologous systems via biochemical and molecular biology methods.
E-mail mysong0823@gmail.com