3M0B

Ru-Porphyrin Protein Scaffolds for Sensing O2

Summary for 3M0B

• Entry DOI: 10.2210/pdb3m0b/pdb
• Related: 1U4H 1U55 1U56 3EEE 3IQB 3LAH 3LAI
• Descriptor: Methyl-accepting chemotaxis protein, [3,3'-(7,12-diethyl-3,8,13,17-tetramethylporphyrin-2,18-diyl-kappa~4~N~21~,N~22~,N~23~,N~24~)dipropanoato(2-)]ruthenium, CARBON MONOXIDE, ... (4 entities in total)
• Functional Keywords: oxygen sensing molecule, signaling protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 1
• Total formula weight: 22741.26

Authors

Winter, M.B.,McLaurin, E.J.,Reece, S.Y.,Olea Jr., C.,Nocera, D.G.,Marletta, M.A. (deposition date: 2010-03-02, release date: 2010-04-14, Last modification date: 2023-09-06)

Primary citation

Winter, M.B.,McLaurin, E.J.,Reece, S.Y.,Olea, C.,Nocera, D.G.,Marletta, M.A.
Ru-porphyrin protein scaffolds for sensing O2.
J.Am.Chem.Soc., 132:5582-5583, 2010

PubMed Abstract: 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.

PubMed: 20373741
DOI: 10.1021/ja101527r

Experimental method

X-RAY DIFFRACTION (2 Å)