用于检测 O2 的 Ru-卟啉蛋白支架
Ru-porphyrin protein scaffolds for sensing O2.
机构信息
Department of Chemistry, QB3 Institute, and Division of Physical Biosciences, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720-3220, USA.
出版信息
J Am Chem Soc. 2010 Apr 28;132(16):5582-3. doi: 10.1021/ja101527r.
Hemoprotein-based scaffolds containing phosphorescent ruthenium(II) CO mesoporphyrin IX (RuMP) are reported here for oxygen (O(2)) sensing in biological contexts. RuMP was incorporated into the protein scaffolds during protein expression utilizing a novel method that we have described previously. A high-resolution (2.00 A) crystal structure revealed that the unnatural porphyrin binds to the proteins in a manner similar to the native heme and does not perturb the protein fold. The protein scaffolds were found to provide unique coordination environments for RuMP and modulate the porphyrin emission properties. Emission lifetime measurements demonstrate a linear O(2) response within the physiological range and precision comparable to commercial O(2) sensors. The RuMP proteins are robust, readily modifiable platforms and display promising O(2) sensing properties for future in vivo applications.
这里报道了一种基于血红素蛋白的支架，其中包含发磷光的钌(II) CO 中卟啉 IX（RuMP），可用于生物环境中的氧气（O(2)）传感。RuMP 是在利用我们之前描述的新方法进行蛋白质表达时掺入到蛋白质支架中的。高分辨率（2.00 A）晶体结构表明，这种非天然卟啉与蛋白质的结合方式类似于天然血红素，并且不会破坏蛋白质折叠。研究发现，蛋白质支架为 RuMP 提供了独特的配位环境，并调节了卟啉的发射特性。发射寿命测量表明，在生理范围内存在线性 O(2)响应，其精度可与商业 O(2)传感器相媲美。RuMP 蛋白是稳健的、易于修饰的平台，并且具有有前途的 O(2)传感性能，可用于未来的体内应用。
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