Excited State Dynamics Can Be Used to Probe Donor-Acceptor Distances for H-Tunneling Reactions Catalyzed by Flavoproteins

作者: Samantha J.O. Hardman , Christopher R. Pudney , Sam Hay , Nigel S. Scrutton

DOI: 10.1016/J.BPJ.2013.10.015

关键词:

摘要: In enzyme systems where fast motions are thought to contribute H-transfer efficiency, the distance between hydrogen donor and acceptor is a very important factor. Sub-angstrom changes in donor-acceptor can have large effect on rate of reaction, so sensitive probe these vital tool our understanding function. this study we use ultrafast transient absorption spectroscopy investigate photoinduced electron transfer rates, which also small distance, coenzyme analog, NAD(P)H4, isoalloxazine center model flavoenzymes morphinone reductase (wild-type selected variants) pentaerythritol tetranitrate (wild-type). It shown that upon addition protein increased. By comparing magnitude increase with existing values for NAD(P)H4-FMN distances, based charge-transfer complex absorbance experimental kinetic isotope reaction data, show method be used as range systems.

参考文章(49)
Christopher C. Page, Christopher C. Moser, Xiaoxi Chen, P. Leslie Dutton, Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. ,vol. 402, pp. 47- 52 ,(1999) , 10.1038/46972
Joris J. Snellenburg, Sergey P. Laptenok, Ralf Seger, Katharine M. Mullen, Ivo H. M. van Stokkum, Glotaran: AJava-Based Graphical User Interface for theRPackageTIMP Journal of Statistical Software. ,vol. 49, pp. 1- 22 ,(2012) , 10.18637/JSS.V049.I03
P. F. Heelis, The photophysical and photochemical properties of flavins (isoalloxazines) Chemical Society Reviews. ,vol. 11, pp. 15- 39 ,(1982) , 10.1039/CS9821100015
Fumio Tanaka, Rong Rujkorakarn, Haik Chosrowjan, Seiji Taniguchi, Noboru Mataga, Analyses of donor–acceptor distance-dependent rates of photo-induced electron transfer in flavoproteins with three kinds of electron transfer theories Chemical Physics. ,vol. 348, pp. 237- 241 ,(2008) , 10.1016/J.CHEMPHYS.2008.03.005
Zachary D. Nagel, Judith P. Klinman, Update 1 of: Tunneling and dynamics in enzymatic hydride transfer. Chemical Reviews. ,vol. 110, ,(2010) , 10.1021/CR1001035
Tina Bhakta, Simon J. Whitehead, John S. Snaith, Tim R. Dafforn, John Wilkie, Sundaresan Rajesh, Scott A. White, J. Baz Jackson, Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries. Biochemistry. ,vol. 46, pp. 3304- 3318 ,(2007) , 10.1021/BI061843R
Antonie J. W. G. Visser, Petra A. W. van den Berg, Nina V. Visser, Arie van Hoek, Harrold A. van den Burg, Derek Parsonage, Al Claiborne, Time-resolved fluorescence of flavin adenine dinucleotide in wild-type and mutant NADH peroxidase: elucidation of quenching sites and discovery of a new fluorescence depolarization mechanism. Journal of Physical Chemistry B. ,vol. 102, pp. 10431- 10439 ,(1998) , 10.1021/JP982141H
Mironel Enescu, Lars Lindqvist, Benoît Soep, Excited‐State Dynamics of Fully Reduced Flavins and Flavoenzymes Studied at Subpicosecond Time Resolution Photochemistry and Photobiology. ,vol. 68, pp. 150- 156 ,(1998) , 10.1111/J.1751-1097.1998.TB02482.X
Daniel H. CRAIG, Terez BARNA, Peter C.E. MOODY, Neil C. BRUCE, Stephen K. CHAPMAN, Andrew W. MUNRO, Nigel S. SCRUTTON, Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin. Biochemical Journal. ,vol. 359, pp. 315- 323 ,(2001) , 10.1042/0264-6021:3590315
Noboru Mataga, Haik Chosrowjan, Seiji Taniguchi, Fumio Tanaka, Nobuo Kido, Masaya Kitamura, Femtosecond fluorescence dynamics of flavoproteins: Comparative studies on flavodoxin, its site-directed mutants, and riboflavin binding protein regarding ultrafast electron transfer in protein nanospaces Journal of Physical Chemistry B. ,vol. 106, pp. 8917- 8920 ,(2002) , 10.1021/JP020574L