TY - JOUR
T1 - Ultrafast Photoinduced Electron Transfer in Green Fluorescent Protein Bearing a Genetically Encoded Electron Acceptor
AU - Lv, Xiaoxuan
AU - Yu, Yang
AU - Zhou, Meng
AU - Hu, Cheng
AU - Gao, Feng
AU - Li, Jiasong
AU - Liu, Xiaohong
AU - Deng, Kai
AU - Zheng, Peng
AU - Gong, Weimin
AU - Xia, Andong
AU - Wang, Jiangyun
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/6/17
Y1 - 2015/6/17
N2 - Electron transfer (ET) is widely used for driving the processes that underlie the chemistry of life. However, our abilities to probe electron transfer mechanisms in proteins and design redox enzymes are limited, due to the lack of methods to site-specifically insert electron acceptors into proteins in vivo. Here we describe the synthesis and genetic incorporation of 4-fluoro-3-nitrophenylalanine (FNO2Phe), which has similar reduction potentials to NAD(P)H and ferredoxin, the most important biological reductants. Through the genetic incorporation of FNO2Phe into green fluorescent protein (GFP) and femtosecond transient absorption measurement, we show that photoinduced electron transfer (PET) from the GFP chromophore to FNO2Phe occurs very fast (within 11 ps), which is comparable to that of the first electron transfer step in photosystem I, from P700∗ to A0. This genetically encoded, low-reduction potential unnatural amino acid (UAA) can significantly improve our ability to investigate electron transfer mechanisms in complex reductases and facilitate the design of miniature proteins that mimic their functions.
AB - Electron transfer (ET) is widely used for driving the processes that underlie the chemistry of life. However, our abilities to probe electron transfer mechanisms in proteins and design redox enzymes are limited, due to the lack of methods to site-specifically insert electron acceptors into proteins in vivo. Here we describe the synthesis and genetic incorporation of 4-fluoro-3-nitrophenylalanine (FNO2Phe), which has similar reduction potentials to NAD(P)H and ferredoxin, the most important biological reductants. Through the genetic incorporation of FNO2Phe into green fluorescent protein (GFP) and femtosecond transient absorption measurement, we show that photoinduced electron transfer (PET) from the GFP chromophore to FNO2Phe occurs very fast (within 11 ps), which is comparable to that of the first electron transfer step in photosystem I, from P700∗ to A0. This genetically encoded, low-reduction potential unnatural amino acid (UAA) can significantly improve our ability to investigate electron transfer mechanisms in complex reductases and facilitate the design of miniature proteins that mimic their functions.
UR - http://www.scopus.com/inward/record.url?scp=84935021929&partnerID=8YFLogxK
U2 - 10.1021/jacs.5b03652
DO - 10.1021/jacs.5b03652
M3 - Article
C2 - 26020364
AN - SCOPUS:84935021929
SN - 0002-7863
VL - 137
SP - 7270
EP - 7273
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 23
ER -