Ultrafast Solvation Dynamics of Human Serum Albumin:  Correlations with Conformational Transitions and Site-Selected Recognition

W, Qiu; Zhang, Luyuan; Okobiah, Oghaghare; Yang, Yi; Wang, Limin; Zhong, Dongping; Zewail, Ahmed H.

doi:10.1021/jp055989w

Cited by 154 publications

(240 citation statements)

References 50 publications

(137 reference statements)

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“…27,28 It has also been demonstrated that the chemical denaturation of the protein allows more bulk type water in the protein cavity, revealing faster time constants in the solvation dynamics. 27,28 A systematic study on the spectroscopy and dynamics of kynurenine in different solvents has been presented by Vauthey et al 16 The usefulness of the probe (kynurenine) as a solvation reporter has also been established. 16 The main excited-state deactivation channel of the probe depends on the interaction of the solvent molecules through hydrogen-bonding ability.…”

Section: Resultsmentioning

confidence: 99%

Toward an Alternative Intrinsic Probe for Spectroscopic Characterization of a Protein

2010

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The intrinsic fluorescent amino acid tryptophan is the unanimous choice for the spectroscopic investigation of proteins. However, several complicacies in the interpretation of tryptophan fluorescence in a protein are inevitable and an alternative intrinsic protein probe is a longstanding demand. In this contribution, we report an electron-transfer reaction in a human transporter protein (HSA) cavity which causes the tryptophan residue (Trp214) to undergo chemical modification to form one of its metabolites kynurenine (Kyn214). Structural integrity upon modification of the native protein is confirmed by dynamic light scattering (DLS) as well as near and far circular dichroism (CD) spectroscopy. Femtosecond-resolved fluorescence transients of the modified protein describe the dynamics of solvent molecules in the protein cavity in both the native and denatured states. In order to establish general use of the probe, we have studied the dipolar interaction of Kyn214 with a surface-bound ligand (crystal violet, CV) of the protein. By using the sensitivity of FRET, we have determined the distance between Kyn214 (donor) and CV (acceptor). Our study is an attempt to explore an alternative intrinsic fluorescence probe for the spectroscopic investigation of a protein. In order to establish the efficacy of the modification technique we have converted the tryptophan residues of other proteins (bovine serum albumin, chymotrypsin and subtilisin Carlsberg) to kynurenine and confirmed their structural integrity. We have also shown that catalytic activity of the enzymes remains intact upon the modification.

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Section: Resultsmentioning

confidence: 99%

Toward an Alternative Intrinsic Probe for Spectroscopic Characterization of a Protein

2010

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“…Both the fluorescence intensity and emission peak (343 nm) reveal that Trp-212 is located close to the protein surface, and thus the crevice (between Domain I and III) Source: adopted from Ref. [29]. must open widely to allow more mobile water molecules into the hydrophobic pocket [29].…”

Section: Ph-dependent Conformational Changesmentioning

confidence: 99%

Exploring the diameter and surface dependent conformational changes in carbon nanotube-protein corona and the related cytotoxicity

Zhao

Lü

Fang

et al. 2015

Journal of Hazardous Materials

130

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“…function-site solvation | ultrafast dynamics | spectral tuning | protein rigidity and flexibility | femtosecond-resolved emission spectra D ynamic solvation in binding and active sites plays a critical role in protein recognition and enzyme reaction, and such local motions optimize spatial configurations and minimize energetic pathways (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). These dynamics involve local constrained protein and trapped-water motions within angstrom distance and occur on ultrafast time scales (6,7,10,11).…”

mentioning

confidence: 99%

“…These dynamics involve local constrained protein and trapped-water motions within angstrom distance and occur on ultrafast time scales (6,7,10,11). Typically, extrinsic dye molecules or synthetic amino acids were used as local optical probes to label function sites, and the local relaxations were observed, ranging from femtoseconds to nanoseconds (5,(12)(13)(14).…”

mentioning

confidence: 99%

Ultrafast solvation dynamics at binding and active sites of photolyases

Chang

Guo

Kao

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Dynamic solvation at binding and active sites is critical to protein recognition and enzyme catalysis. We report here the complete characterization of ultrafast solvation dynamics at the recognition site of photoantenna molecule and at the active site of cofactor/ substrate in enzyme photolyase by examining femtosecondresolved fluorescence dynamics and the entire emission spectra. With direct use of intrinsic antenna and cofactor chromophores, we observed the local environment relaxation on the time scales from a few picoseconds to nearly a nanosecond. Unlike conventional solvation where the Stokes shift is apparent, we observed obvious spectral shape changes with the minor, small, and large spectral shifts in three function sites. These emission profile changes directly reflect the modulation of chromophore's excited states by locally constrained protein and trapped-water collective motions. Such heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA. Such unusual solvation and synergetic dynamics should be general in function sites of proteins.function-site solvation | ultrafast dynamics | spectral tuning | protein rigidity and flexibility | femtosecond-resolved emission spectra D ynamic solvation in binding and active sites plays a critical role in protein recognition and enzyme reaction, and such local motions optimize spatial configurations and minimize energetic pathways (1-11). These dynamics involve local constrained protein and trapped-water motions within angstrom distance and occur on ultrafast time scales (6,7,10,11). Typically, extrinsic dye molecules or synthetic amino acids were used as local optical probes to label function sites, and the local relaxations were observed, ranging from femtoseconds to nanoseconds (5,(12)(13)(14). Such labeling of bulky dye molecules usually induces significant local perturbations, and direct characterization with intrinsic chromophores in proteins eliminates those interferences and reveals intact environment responses (4, 7, 15-21), as recently examined in green fluorescence proteins (21). We have recently studied a series of flavoproteins using intrinsic flavin molecule as the optical probe (10, 22, 23) and especially found the important functional role of local solvation in photolyase (10).Photolyase, a flavoprotein and a photoenzyme, repairs damaged DNA caused by UV irradiation. Two types of structurally similar photolyases are specific for two major UV-induced DNA lesions of cyclobutane pyrimidine dimer (CPD) and (6-4) photoproduct (24). The CPD photolyase contains two noncovalently bound chromophores, a pterin molecule in the form of methenyltetrahydrofolate (MTHF) in the binding site as the photoantenna for energy efficiency and a fully reduced flavin adenine dinucleotide (FADH − ) at the active site as the catalytic cofactor for repair of d...

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Ultrafast Solvation Dynamics of Human Serum Albumin: Correlations with Conformational Transitions and Site-Selected Recognition

Abstract: The typical fs-resolved fluorescence transients are shown in Figure 2-

Cited by 154 publications

References 50 publications

Toward an Alternative Intrinsic Probe for Spectroscopic Characterization of a Protein

Toward an Alternative Intrinsic Probe for Spectroscopic Characterization of a Protein

Exploring the diameter and surface dependent conformational changes in carbon nanotube-protein corona and the related cytotoxicity

Ultrafast solvation dynamics at binding and active sites of photolyases

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