氨基酸复合分解同位素:用于追踪环境中循环的含义
Corday R Selden1,2, Kathrin Schilling3, Anirban Basu3
1Department of Marine and Coastal Sciences, Rutgers University, New Brunswick, New Jersey 08901, United States.
概括
(Ni) 的稳定同位素在与氨基酸和结合时分化. 谷氨酸和氨酸倾向于重型60Ni,而氨酸显示最小的转移,揭示了Ni同位素分离的机制.
科学领域:
- 生物地质化学生物地质化学
- 地质化学 地质化学
- 生物物理学的生物物理.
背景情况:
- (Ni) 是许多蛋白质中的重要辅因子.
- 稳定的同位素在生物系统中表现出分化,但机制尚不清楚.
研究的目的:
- 调查关键氨基酸 (谷氨酸,胺,氨酸) 结合期间的Ni同位素分离.
- 确定连接体类型对Ni同位素分割的影响.
- 在模仿金属蛋白结合位点的中探索Ni同位素分离.
主要方法:
- 均衡的多南透析用于分离自由和结合的.
- 多采集器感应合等离子体质谱 (MC-ICP-MS) 用于同位素分析.
- 与氨基酸和一个模型的实验性结合.
主要成果:
- 氨酸和氨酸结合优选丰富的重型60Ni (Δ60/58Ni = +0.80‰和+1.27‰,分别).
- 伊斯蒂丁结合显示了可以忽略不计的Ni同位素分离 (Δ60/58Ni = -0.12‰).
- 一个模型也优先结合重型60Ni (Δ60/58Ni = +0.74‰),与连接体效应一致.
结论:
- 连接物类型显著控制结合过程中的Ni同位素分离.
- 观察到的分化与协调化学相关,提供了机械学的洞察力.
- 这项研究促进了对生物和环境环境中的Ni同位素分离驱动因素的理解.
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