Ru-Porphyrin Protein Scaffolds for Sensing O2

被引：54

作者：

Winter, Michael B. ^{[1
,2
,3
]}

McLaurin, Emily J. ^{[4
]}

Reece, Steven Y. ^{[1
,2
,3
]}

Olea, Charles, Jr. ^{[1
,2
,3
]}

Nocera, Daniel G. ^{[4
]}

Marletta, Michael A. ^{[1
,2
,3
]}

机构：

[1] Univ Calif Berkeley, Lawrence Berkeley Lab, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Dept Mol & Cell Biol, Inst QB3, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Phys Biosci, Berkeley, CA 94720 USA

[4] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2010年 / 132卷 / 16期

基金：

美国国家卫生研究院;

关键词：

PHOSPHORESCENCE; MYOGLOBIN; DIOXYGEN; OXYGEN;

D O I：

10.1021/ja101527r

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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 angstrom) 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.

引用

页码：5582 / +

页数：4

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