UV resonance Raman investigation on detection of higher order structural changes of heme proteins and elucidation of functional regulation mechanism

2014 Fiscal Year Final Research Report

• Project/Area Number: 24350086
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Chemistry related to living body
• Research Institution: University of Hyogo
• Principal Investigator: KITAGAWA Teizo 兵庫県立大学, 生命理学研究科, 名誉教授 (40029955)
• Co-Investigator(Kenkyū-buntansha): OGURA Takashi 兵庫県立大学, 生命理学研究科, 教授 (70183770) ; NAGATOMO Shigenori 筑波大学, 数理物質科学研究科, 講師 (80373190)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 生物物理 / 蛋白質 / シグナル伝達 / 生体分子 / 分子認識 / 振動分光 / 共鳴ラマン散乱

Outline of Final Research Achievements

Cavity mutant human Hb, which lacks the Fe-His bond in either the α or β subunit but can bind four O2 molecules, was prepared. Its oxygen binding curve was determined, and higher order structural changes upon O2 binding were investigated with 1H NMR, V- and UV-resonance Raman, and nearUV CD spectra. Spectroscopic measurements revealed that the quaternary structure change did not occur upon ligand binding. The absence of Fe-His bond in α froze Hb in T while that of β raised the affinity of α. Resonance Raman spectra of NO sensor protein, mammalian sGC and its model protein, bacterial H-NOX, were investigated.

Free Research Field

生物物理化学