Ultrafast internal conversion dynamics of bilirubin bound to UnaG and its N57A mutant-Reference-Cited by-同舟云学术

Ultrafast internal conversion dynamics of bilirubin bound to UnaG and its N57A mutant

Published:2019 Issue:5 Volume:21 Page:2365-2371
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Cao Xiaodan¹²³⁴^ORCID,Zhang Changcheng⁵⁶³⁴,Gao Ziheng⁵⁶³⁴,Liu Yangyi¹²³⁴,Zhao Yuzheng⁵⁶³⁴,Yang Yi⁵⁶³⁴^ORCID,Chen Jinquan¹²³⁴⁷^ORCID,Jimenez Ralph⁸⁹¹⁰¹¹¹²^ORCID,Xu Jianhua¹²³⁴⁷^ORCID

Affiliation:

1. State Key Laboratory of Precision Spectroscopy

2. East China Normal University

3. Shanghai

4. China

5. School of Pharmacy

6. East China University of Science and Technology

7. Collaborative Innovation Center of Extreme Optics

8. JILA

9. NIST and University of Colorado

10. Boulder

11. USA

12. Department of Chemistry and Biochemistry

Abstract

High fluorescence quantum yield of BR in UnaG is due to direct hydrogen bonds to the endo-vinyl dipyrrinone moiety.

Funder

National Natural Science Foundation of China

Division of Physics

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C8CP07553K

Reference28 articles.

1. Exploiting the cyanobacterial light-harvesting machinery for developing fluorescent probes

2. A Bilirubin-Inducible Fluorescent Protein from Eel Muscle

3. Blue protein with red fluorescence

4. A far-red fluorescent protein evolved from a cyanobacterial phycobiliprotein

5. Bright monomeric near-infrared fluorescent proteins as tags and biosensors for multiscale imaging

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