Protozoan Myoglobin : Its structure, function and evolution

原生动物肌红蛋白：其结构、功能和进化

• 批准号: 04454022
• 负责人: SHIKAMA Keiji
• 金额: $ 3.78万
• 依托单位: Tohoku University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (B)
• 财政年份: 1992
• 资助国家: 日本
• 起止时间: 1992 至 1994
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-04454022/
• 关键词: hemoglobin; Myoglobin; Protozoan; Primary Structure; CD; Autoisdebon; helix content; hewiohrome; hemoglobin; Myoglobin; Protozoa; Primary structure; CD(MCD); Autoxidation; helix content; hemichrome; 分子進化; 呼吸生理; 酸素; 分子構造

A hemoglobin-like protein is present in some of the single-celled organisms, but its structure is quite different from that of mammalian myoglobin or hemoglobin. For instance, a protozoan myoglobin isolated from Paramecium caudatum consists of 116 amino acid residues, so that this contracted form is nearly two thirds of sperm whale myoglobin. Yeast hemoglobin from Candida norvegensis, on the other hand, is composed of a single polypeptide chain of 387 amino acid residues, but of two distinct domains carrying different functions ; that is the N-terminal, heme-containing region and the C-terminal, FAD-containing reductase domain.hemoglobin/myoglobin/protozoa (Paramecium caudatum) /yeast (Candida norvegensis) /amino acid sequence

一种血红蛋白样蛋白存在于某些单细胞生物中，但其结构与哺乳动物的肌红蛋白或血红蛋白大不相同。例如，从尾草笋虫中分离出来的一种原生动物的肌红蛋白，是由一百一十六个氨基酸残基组成的，因此，这种收缩的形式差不多是抹香鲸肌红蛋白的三分之二。另一方面，来自诺维假丝酵母的酵母血红蛋白是由387个氨基酸残基组成的单一多肽链，但具有两个不同的功能域；即n端含血红素区域和c端含fad还原酶区域。血红蛋白/肌红蛋白/原生动物（尾草履虫）/酵母菌（诺维根假丝酵母）/氨基酸序列

项目成果

M.Fukuda: "Polymorphic Hb from a midge larua can be divided into two different types." Biochim.Biophys.Acta. 1157. 185-191 (1993)

M.Fukuda：“来自蠓的多态性 Hb 可以分为两种不同的类型。”

K.Akiyama: "The pH-dependent swinging-out of the distal histidine residul" Biochim.Biophys.Acta. 1208. 306-309 (1994)

K.Akiyama：“远端组氨酸残基的 pH 依赖性摆动”Biochim.Biophys.Acta。

G.Tajima: "Decomposition of Hydrogen perokide by metmyoglobin." Int.J.Biochemistry. 25. 101-105 (1993)

G.Tajima：“高铁肌红蛋白分解过氧化氢。”

A.MATSUOKA: "The Soret magnetic circular elichroism of ferric high-Apin myoglobine" Eur, g. Biochem.210. 337-341 (1992)

A.MATSUOKA：“铁高 Apin 肌红蛋白的 Soret 磁圆 elichroism”Eur，g。

K.Akiyama, M.Fukuda, N.Kobayashi, A,Matsuoka and K.SHIKAMA: "The pH-dependent shinging out of the distal histidine residue in ferric hemoglobin of a midge larva (T.akamusi)" Biochim. Biophys. Acta. 1208. 306-309 (1994)

K.Akiyama、M.Fukuda、N.Kobayashi、A、Matsuoka 和 K.SHIKAMA：“蠓幼虫 (T.akamusi) 铁血红蛋白远端组氨酸残基的 pH 依赖性脱落”Biochim。