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| Type |
Poster Presentation |
| Area |
Inorganic Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
INOR.P-49 |
| Subject |
Structural and kinetic studies of MMOR ; An EPR Study |
| Authors |
Hansol Jeong, Sugyeong Hong, Seung Jae Lee1,*, Sun Hee Kim2,*
Department of Chemistry and Nano Science, Ewha Womans University, Korea
1Department of Chemistry, Chonbuk National University, Korea
2Western Seoul Center, Korea Basic Science Institute, Korea
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| Abstract |
Methane monooxygenase (MMO) is able to turn into inert methane to methanol. Therefore, it is gaining significant attention due to its crucial role in global carbon cycle and to hinder greenhouse effect by removing methane from the atmosphere. Moreover, the product of MMO’s methane oxidation reaction, methanol, is also able to use alternative energy. The soluble form of MMO has three components; (I) Hydroxylase (MMOH), (II) Reductase (MMOR), and (III) β-unit (MMOB). MMOR consists of flavin adenine dinucleotide (FAD) and [2Fe-2S]2+ (III,III). It is known that MMOR is involved in electron transfer to MMOH. However, the role of MMOR is not clarified yet. To elucidate electron transfer pathway of MMOR, we probed the structure and kinetics of electron transfer of MMOR by CW-EPR, pulsed EPR spectroscopy. In addition, we have investigated the effect of MMOB on MMOR in terms of structure and kinetics. To study EPR-silent MMOR at the resting state, we have performed chemical reduction to make it EPR-visible. In addition to confirm the results of chemical reduction experiments, we have carried out cryo-reduction experiments as well. Thus, EPR studies coupled with cryo-reduction and annealing techniques, will provide an essential clue to comprehend unknown the electron transfer pathway of MMOR. |
| E-mail |
hsjeong94@kbsi.re.kr |
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120th General Meeting of the KCS