1988 Fiscal Year Final Research Report Summary

Correlation between dynamic structure and catalytic function of flavoenzymes

Research Project

Project/Area Number	62570110
Research Category	Grant-in-Aid for General Scientific Research (C)
Allocation Type	Single-year Grants
Research Field	General medical chemistry
Research Institution	Tokushima University
Principal Investigator	AKI Kenji Institute for Enzyme Research, Professor, 酵素制御学部門, 教授 (20035405)
Co-Investigator(Kenkyū-buntansha)	MATSUSHIMA Akemi Institute for Enzyme Research, Technical assistant, 酵素制御学部門, 教務員 (70116862) MAEDA Kazuko Institute for Enzyme Research, Research assistant, 酵素制御学部門, 助手 (60116879)
Project Period (FY)	1987 – 1988
Keywords	flavoenzyme / domain / oxidation-reduction / limited proteolysis / fluorescence depolarization and lifetime / circular dichroism / 電子スピン共鳴
Research Abstract	Flavoenzymes, lipoate dehydrogenase and flavocytochrome B_2 was studied on correlation between the dynamic structure and catalytic function. The protein structures were determined by circular dichroism and fluorescence. The catalytic functions were measured by enzyme kinetics and electron spin resonace. Lipoate dehydrogenase was composed of four domains. NAD-binding domain fluctuated to elevate efficiency of electron transfer. Flavocytochrome B_2 was composed of two domains, flavin-binding domain which had a diaphorase activity and heme-binding domain. complex formation of both domains suppressed a diaphorase activity and induced a lactate dehydrogenase activity.