Document Detail


Fourier-transform infrared study of the photoactivation process of Xenopus (6-4) photolyase.
MedLine Citation:
PMID:  22747528     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Photolyases (PHRs) are blue light-activated DNA repair enzymes that maintain genetic integrity by reverting UV-induced photoproducts into normal bases. The flavin adenine dinucleotide (FAD) chromophore of PHRs has four different redox states: oxidized (FAD(ox)), anion radical (FAD(•-)), neutral radical (FADH(•)), and fully reduced (FADH(-)). We combined difference Fourier-transform infrared (FTIR) spectroscopy with UV-visible spectroscopy to study the detailed photoactivation process of Xenopus (6-4) PHR. Two photons produce the enzymatically active, fully reduced PHR from oxidized FAD: FAD(ox) is converted to semiquinone via light-induced one-electron and one-proton transfers and then to FADH(-) by light-induced one-electron transfer. We successfully trapped FAD(•-) at 200 K, where electron transfer occurs but proton transfer does not. UV-visible spectroscopy following 450 nm illumination of FAD(ox) at 277 K defined the FADH(•)/FADH(-) mixture and allowed calculation of difference FTIR spectra among the four redox states. The absence of a characteristic C=O stretching vibration indicated that the proton donor is not a protonated carboxylic acid. Structural changes in Trp and Tyr are suggested by UV-visible and FTIR analysis of FAD(•-) at 200 K. Spectral analysis of amide I vibrations revealed structural perturbation of the protein's β-sheet during initial electron transfer (FAD(•-) formation), a transient increase in α-helicity during proton transfer (FADH(•) formation), and reversion to the initial amide I signal following subsequent electron transfer (FADH(-) formation). Consequently, in (6-4) PHR, unlike cryptochrome-DASH, formation of enzymatically active FADH(-) did not perturb α-helicity. Protein structural changes in the photoactivation of (6-4) PHR are discussed on the basis of these FTIR observations.
Authors:
Daichi Yamada; Yu Zhang; Tatsuya Iwata; Kenichi Hitomi; Elizabeth D Getzoff; Hideki Kandori
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-07-13
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-07-24     Completed Date:  2012-10-01     Revised Date:  2012-11-01    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5774-83     Citation Subset:  IM    
Affiliation:
Department of Frontier Materials, Nagoya Institute of Technology, Nagoya 466-8555, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Deoxyribodipyrimidine Photo-Lyase / chemistry,  metabolism*
Flavin-Adenine Dinucleotide / chemistry,  metabolism*
Light
Oxidation-Reduction
Protein Structure, Secondary
Spectrophotometry, Ultraviolet
Spectroscopy, Fourier Transform Infrared / methods
Xenopus / metabolism*
Xenopus Proteins / chemistry,  metabolism*
Grant Support
ID/Acronym/Agency:
GM37684/GM/NIGMS NIH HHS; R01 GM037684/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Xenopus Proteins; 146-14-5/Flavin-Adenine Dinucleotide; EC 4.1.99.3/Deoxyribodipyrimidine Photo-Lyase

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