한국생물물리학회:학술대회논문집 (Proceedings of the Korean Biophysical Society Conference)
- 한국생물물리학회 2002년도 제9회 학술 발표회 프로그램과 논문초록
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- Pages.18-18
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- 2002
$^{13}C$ and $^{57}Fe$ END OR of Nitrogenase: Can it Tell the Substrate-Binding Site in the Active Site?
초록
Nitrogenase, comprised of the MoFe and Fe proteins, catalyzes the reduction of dinitrogen to ammonia at ambient temperature and pressure. The MoFe protein contains two metal centers, the P-cluster (Fe8S7-8) and the FeMo-cofactor (Fe7S9:homocitrate), the substrate binding site. Despite the availability of the crystal structure of the MoFe protein, suprisingly little is known about the molecular details of catalysis at the active site, and no small-molecule substrate or inhibitor had ever been shown to directly interact with a protein-bound cluster of the functioning enzyme, until our electron-nuclear double resonance(ENDOR) study of CO-inhibited nitrogenase.(omitted)
키워드