Genetic Engineering of Oxygen Affinity of Bacterial Hemoglobin: Effects on Hemoglobin Structure, Respiration, and Other Cellular Processes

细菌血红蛋白氧亲和力的基因工程：对血红蛋白结构、呼吸和其他细胞过程的影响

• 批准号: 9910356
• 负责人: Benjamin Stark
• 金额: $ 37.48万
• 依托单位: Illinois Institute of Technology
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-03-01 至 2004-02-29
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9910356&HistoricalAwards=false
• 关键词: Genetic; Engineering; Oxygen; Affinity; Bacterial

9910356WebsterVitreoscilla produces hemoglobin that displays an unusually high rate of oxygen dissociation. Although the function of VHb in its natural host is not known, evidence suggests that it facilitates respiration under hypoxic conditions by funneling oxygen to the terminal oxidases. Biophysical characteristics and oxygen binding properties of selected mutants of VHb will be analyzed. The crystal structure of hemoglobin (VHb) obtained from the aerobic bacterium Vitreoscilla is available thus facilitating this research. These studies will help assess whether predicted structural changes from each of the site-directed mutations have occurred and how changes in the oxygen binding affinity alter respiratory activity and oxygen metabolism of microbial systems. VHb function in the native organism will be evaluated also using a vgb (gene) knockout mutation (to eliminate VHb) to determine the role of VHb on growth, respiration and ATP synthesis, especially under hypoxic conditions.

9910356 WebsterVitrechina产生的血红蛋白显示出异常高的氧解离速率。 虽然VHb在其天然宿主中的功能尚不清楚，但有证据表明，它通过将氧转运至末端氧化酶而促进缺氧条件下的呼吸。 将分析所选VHb突变体的生物物理特性和氧结合特性。从需氧细菌Vitrebella获得的血红蛋白（VHb）的晶体结构是可用的，从而促进了这项研究。这些研究将有助于评估每个定点突变是否发生了预测的结构变化，以及氧结合亲和力的变化如何改变微生物系统的呼吸活性和氧代谢。 还将使用vgb（基因）敲除突变（以消除VHb）来评估天然生物体中的VHb功能，以确定VHb对生长、呼吸和ATP合成的作用，特别是在缺氧条件下。