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Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase–luciferin complex 荧光素-荧光素复合物中配体的光激发引起酶色氨酸荧光的瞬时增强
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<378::AID-BSPY7>3.0.CO;2-Q
L. Yu. Brovko, E. Yu. Cherednikova, A. Yu. Chikishev, E. I. Dementieva, N. I. Koroteev, N. N. Ugarova
{"title":"Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase–luciferin complex","authors":"L. Yu. Brovko,&nbsp;E. Yu. Cherednikova,&nbsp;A. Yu. Chikishev,&nbsp;E. I. Dementieva,&nbsp;N. I. Koroteev,&nbsp;N. N. Ugarova","doi":"10.1002/(SICI)1520-6343(1999)5:6<378::AID-BSPY7>3.0.CO;2-Q","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<378::AID-BSPY7>3.0.CO;2-Q","url":null,"abstract":"<p>An experiment was proposed and accomplished that was based on the hypothesis of the dissociation of the luciferase–luciferin complex in photoexcitation. A pump–probe experiment was performed with the use of picosecond laser pulses and was based on the effect of quenching of enzyme tryptophan fluorescence caused by luciferin binding. A photoinduced increase of the tryptophan fluorescence intensity was detected. Experimental results were interpreted on the basis of the assumptions on photoinduced dissociation of the luciferin–luciferase complex and Forster energy transfer from tryptophan to luciferin. Under the assumption on the photoinduced dissociation and stationary quenching of tryptophan fluorescence the rate of propagation of the conformational changes in the protein caused by the complex dissociation was estimated to be &gt;20 m/s. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 378–384, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"378-384"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<378::AID-BSPY7>3.0.CO;2-Q","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21461870","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1
Biological effects of rare earth protein complexes: Influence of lanthanide ions Eu3+, Tb3+ on secondary structure of calmodulins 稀土蛋白复合物的生物学效应:镧系离子Eu3+、Tb3+对钙调素二级结构的影响
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-%23
Yuan-Yuan Song, Yi-Zhuang Xu, Shi-Fu Weng, Li-Bo Wang, Xiao-Feng Li, Ting-Fang Zhang, Jin-Guang Wu
{"title":"Biological effects of rare earth protein complexes: Influence of lanthanide ions Eu3+, Tb3+ on secondary structure of calmodulins","authors":"Yuan-Yuan Song,&nbsp;Yi-Zhuang Xu,&nbsp;Shi-Fu Weng,&nbsp;Li-Bo Wang,&nbsp;Xiao-Feng Li,&nbsp;Ting-Fang Zhang,&nbsp;Jin-Guang Wu","doi":"10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-%23","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1999)5:6<371::AID-BSPY6>3.0.CO;2-%23","url":null,"abstract":"<p>The secondary structure of four kinds of calmodulins (CaMs; i.e., <i>Brassica campestris</i> pollen CaM, bovine brain CaM, earthworm calcium binding protein, and earthworm new calcium binding protein) in thin films are determined by the FTIR resolution enhanced technique and curve fitting. The variation in the secondary structure of CaM upon its binding with Ca<sup>2+</sup>, Eu<sup>3+</sup>, and Tb<sup>3+</sup>, the assay of phosphodiesterase enzyme, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis are also investigated. The effect of lanthanide ions on the conformation of CaM are described. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 371–377, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"371-377"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137635139","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Alteration of infrared spectrum of serum transferrin by iron binding and lowered pH 铁结合及降低pH对血清转铁蛋白红外光谱的影响
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<325::AID-BSPY1>3.0.CO;2-P
Robert J. Donohoe
{"title":"Alteration of infrared spectrum of serum transferrin by iron binding and lowered pH","authors":"Robert J. Donohoe","doi":"10.1002/(SICI)1520-6343(1999)5:6<325::AID-BSPY1>3.0.CO;2-P","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<325::AID-BSPY1>3.0.CO;2-P","url":null,"abstract":"<p>Difference infrared spectra are reported for human serum transferrin in D<sub>2</sub>O as a function of iron binding or increased acidity. Spectral features detected as iron is bound at high pH include difference bands that are indicative of reduced solvent exposure and binding site ligation. More extensive spectral alterations, some of which indicate titration of carboxylic acid groups, are induced in the apo protein by lowering the pH in a manner consistent with that entailed in endocytosis. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 325–327, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"325-327"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<325::AID-BSPY1>3.0.CO;2-P","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463163","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Vibrational spectroscopic study of glutathione complexation in aqueous solutions 水溶液中谷胱甘肽络合的振动光谱研究
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<328::AID-BSPY2>3.0.CO;2-J
Michel Picquart, Lydie Grajcar, Marie Hélène Baron, Zohreh Abedinzadeh
{"title":"Vibrational spectroscopic study of glutathione complexation in aqueous solutions","authors":"Michel Picquart,&nbsp;Lydie Grajcar,&nbsp;Marie Hélène Baron,&nbsp;Zohreh Abedinzadeh","doi":"10.1002/(SICI)1520-6343(1999)5:6<328::AID-BSPY2>3.0.CO;2-J","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<328::AID-BSPY2>3.0.CO;2-J","url":null,"abstract":"<p>A spectroscopic study of glutathione (GSH) and glutathione disulfide (GSSG) has been performed using Fourier-transformed infrared absorption and Raman scattering in order to pinpoint the sites of complexation of these two species with water and particularly with H<sub>2</sub>O<sub>2</sub>. Molecules of GSH and GSSG were studied in KBr pellets, and in aqueous solutions of H<sub>2</sub>O, D<sub>2</sub>O, and H<sub>2</sub>O with H<sub>2</sub>O<sub>2</sub> (1 mol L<sup>−1</sup>) to characterize the specific influence of the solvent molecules. A time-resolved Raman study was performed for GSH/H<sub>2</sub>O<sub>2</sub> in aqueous solution at 1 : 1 molar ratio in order to observe the formation of GSSG and to discuss the mechanism of this redox reaction. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 328–337, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"328-337"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<328::AID-BSPY2>3.0.CO;2-J","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463164","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 38
Resonance Raman spectroscopy and quantum chemical modeling studies of protein–astaxanthin interactions in α-crustacyanin (major blue carotenoprotein complex in carapace of lobster, Homarus gammarus) 共振拉曼光谱和量子化学建模研究α-甲壳青素(龙虾甲壳中主要的蓝胡萝卜素-蛋白复合物)中蛋白质-虾青素相互作用
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<358::AID-BSPY5>3.0.CO;2-1
R. J. Weesie, J. C. Merlin, H. J. M. De Groot, G. Britton, J. Lugtenburg, F. J. H. M. Jansen, J. P. Cornard
{"title":"Resonance Raman spectroscopy and quantum chemical modeling studies of protein–astaxanthin interactions in α-crustacyanin (major blue carotenoprotein complex in carapace of lobster, Homarus gammarus)","authors":"R. J. Weesie,&nbsp;J. C. Merlin,&nbsp;H. J. M. De Groot,&nbsp;G. Britton,&nbsp;J. Lugtenburg,&nbsp;F. J. H. M. Jansen,&nbsp;J. P. Cornard","doi":"10.1002/(SICI)1520-6343(1999)5:6<358::AID-BSPY5>3.0.CO;2-1","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<358::AID-BSPY5>3.0.CO;2-1","url":null,"abstract":"<p>Resonance Raman spectroscopy and quantum chemical calculations were used to investigate the molecular origin of the large redshift assumed by the electronic absorption spectrum of astaxanthin in α-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, <i>Homarus gammarus</i>. Resonance Raman spectra of α-crustacyanin reconstituted with specifically <sup>13</sup>C-labeled astaxanthins at the positions 15, 15,15′, 14,14′, 13,13′, 12,12′, or 20,20′ were recorded. This approach enabled us to obtain information about the effect of the ligand–protein interactions on the geometry of the astaxanthin chromophore in the ground electronic state. The magnitude of the downshifts of the CC stretching modes for each labeled compound indicate that the main perturbation on the central part of the polyene chain is not homogeneous. In addition, changes in the 1250–1400 cm<sup>−1</sup> spectral range indicate that the geometry of the astaxanthin polyene chain is moderately changed upon binding to the protein. Semiempirical quantum chemical modeling studies (Austin method 1) show that the geometry change cannot be solely responsible for the bathochromic shift from 480 to 632 nm of protein-bound astaxanthin. The calculations are consistent with a polarization mechanism that involves the protonation or another interaction with a positive ionic species of comparable magnitude with both ketofunctionalities of the astaxanthin-chromophore and support the changes observed in the resonance Raman and visible absorption spectra. The results are in good agreement with the conclusions that were drawn on the basis of a study of the charge densities in the chromophore in α-crustacyanin by solid-state NMR spectroscopy. From the results the dramatic bathochromic shift can be explained not only from a change in the ground electronic state conformation but also from an interaction in the excited electronic state that significantly decreases the energy of the π-antibonding CO orbitals and the HOMO–LUMO gap. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 358–370, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"358-370"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<358::AID-BSPY5>3.0.CO;2-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463167","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 16
Certain species of the Proteobacteria possess unusual bacteriochlorophyll a environments in their light-harvesting proteins 某些种类的变形杆菌在它们的捕光蛋白中具有不寻常的细菌叶绿素a环境
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<338::AID-BSPY3>3.0.CO;2-D
Andrew Gall, Vladimir Yurkov, André Vermeglio, Bruno Robert
{"title":"Certain species of the Proteobacteria possess unusual bacteriochlorophyll a environments in their light-harvesting proteins","authors":"Andrew Gall,&nbsp;Vladimir Yurkov,&nbsp;André Vermeglio,&nbsp;Bruno Robert","doi":"10.1002/(SICI)1520-6343(1999)5:6<338::AID-BSPY3>3.0.CO;2-D","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<338::AID-BSPY3>3.0.CO;2-D","url":null,"abstract":"<p>In this work, we have examined, using Fourier-transform Raman (FT-R) spectroscopy, the bacteriochlorophyll <i>a</i> (BChl <i>a</i>) binding sites in light-harvesting (LH) antennae from different species of the <i>Proteobacteria</i> that exhibit unusal absorption properties. While the LH1 complexes from <i>Erythromicrobium</i> (<i>E</i>.)<i> ramosum</i> (RC-B871) and<i> Rhodospirillum centenum</i> (B875) present classic FT-R spectra in the carbonyl high-frequency region, we show that in the blue-shifted LH1 complex, absorbing at 856 nm, from <i>Roseococcus thiosulfatophilus</i>, as well as in the B798–832 LH2 from <i>E</i>.<i> ramosum</i>, or in the B830 complex from the obligate phototrophic bacterium <i>Chromatium purpuratum</i>, some H-bonds between the acetyl carbonyl of the BChl <i>a</i> and the surrounding protein are missing. The molecular mechanisms responsible for the unusual absorption of these complexes are thus similar to those responsible for tuning of the absorption of the LH2 complexes between 850 and 820 nm. Furthermore, our results suggest that the binding pocket of the monomeric BChl in the LH2 from <i>E</i>.<i> ramosum</i> is different from that of <i>Rps</i>.<i> acidphila</i> or <i>Rb</i>.<i> sphaeroides</i>. The FT-R spectra of <i>Chromatium purpuratum</i> indicate that, in contrast with every LH2 complex previously studied by FT-R spectroscopy, no free-from-interaction keto groupings exist in this complex. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 338–345, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"338-345"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<338::AID-BSPY3>3.0.CO;2-D","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463165","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 5
Relationship between altered structure and photochemistry in mutant reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin 细菌叶绿素取代光活性细菌叶绿素的突变反应中心中结构改变与光化学的关系
Biospectroscopy Pub Date : 1999-12-02 DOI: 10.1002/(SICI)1520-6343(1999)5:6<346::AID-BSPY4>3.0.CO;2-9
Kazimierz Czarnecki, Agnes Cua, Christine Kirmaier, Dewey Holten, David F. Bocian
{"title":"Relationship between altered structure and photochemistry in mutant reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin","authors":"Kazimierz Czarnecki,&nbsp;Agnes Cua,&nbsp;Christine Kirmaier,&nbsp;Dewey Holten,&nbsp;David F. Bocian","doi":"10.1002/(SICI)1520-6343(1999)5:6<346::AID-BSPY4>3.0.CO;2-9","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:6<346::AID-BSPY4>3.0.CO;2-9","url":null,"abstract":"<p><i>Q</i><sub><i>y</i></sub>-excitation resonance Raman (RR) spectra are reported for two mutant reaction centers (RCs) from <i>Rhodobacter capsulatus</i> in which the photoactive bacteriopheophytin (BPh<sub>L</sub>) is replaced by a bacteriochlorophyll (BChl) molecule, designated β. The pigment change in both mutants is induced via introduction of a histidine residue near the photoactive cofactor. In one mutant, L(M212)H, the histidine is positioned over the core of the cofactor and serves as an axial ligand to the Mg<sup>+2</sup> ion. In the other mutant, F(L121)H/F(L97)V, the histidine is positioned over ring V of the cofactor, which is nominally too distant to permit bonding to the Mg<sup>+2</sup> ion. The salient observations are as follows: (1) The β cofactor in F(L121)H/F(L97)V RCs is a five-coordinate BChl molecule. However, there is no evidence for the formation of a Mg-His bond. This bond is either much weaker than in the L(M212)H RCs or completely absent, the latter implying coordination by an alternative ligand. The different axial ligation for β in the F(L121)H/F(L97)V versus L(M212)H RCs in turn leads to different conformations of the BChl macrocycles. (2) The C<sub>9</sub>-keto group of β in F(L121)H/F(L97)V RCs is free of hydrogen bonding interactions, unlike the L(M212)H RCs in which the C<sub>9</sub>-keto of β is hydrogen bonded to Glu L104. The interactions between other peripheral substituents of β and the protein are also different in the F(L121)H/F(L97)V RCs versus L(M212)H RCs. Accordingly, the position and orientation of β in the protein is different in the two β-containing RCs. Nonetheless, previous studies have shown that the primary electron transfer reactions are very similar in the two mutants but differ in significant respects compared to wild-type RCs. Collectively, these observations indicate that changes in the conformation of a photoactive tetrapyrrole macrocycle or its interactions with the protein do not necessarily lead to significantly perturbed photochemistry and do not underlie the altered primary events in beta-type RCs. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 346–357, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 6","pages":"346-357"},"PeriodicalIF":0.0,"publicationDate":"1999-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:6<346::AID-BSPY4>3.0.CO;2-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21463166","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance Raman spectroscopy 用共振拉曼光谱研究了嗜热热菌ba3氧化酶的活性位点结构
Biospectroscopy Pub Date : 1999-09-22 DOI: 10.1002/(SICI)1520-6343(1999)5:5+<S53::AID-BSPY6>3.0.CO;2-2
S. Gerscher, P. Hildebrandt, G. Buse, T. Soulimane
{"title":"The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance Raman spectroscopy","authors":"S. Gerscher,&nbsp;P. Hildebrandt,&nbsp;G. Buse,&nbsp;T. Soulimane","doi":"10.1002/(SICI)1520-6343(1999)5:5+<S53::AID-BSPY6>3.0.CO;2-2","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:5+<S53::AID-BSPY6>3.0.CO;2-2","url":null,"abstract":"<p>The <i>ba</i><sub>3</sub> cytochrome oxidase from <i>Thermus thermophilus</i> was studied by resonance Raman spectroscopy. The component spectra of both heme groups were determined by using different excitation wavelengths. In the ferric state the heme <i>a</i><sub>3</sub> group reveals resonance Raman marker bands characteristic for two high spin species with the heme iron in an in-plane and an out-of-plane configuration that reflects a coordination equilibrium. This equilibrium obviously results from protonation of one of the axial ligands that is ascribed to a hydroxide. Coordination by its protonated form, a water molecule, may be too weak to keep the heme iron in the porphyrin plane. The corresponding Fe-OH<sub>2</sub> stretching mode was attributed to a weak H/D-sensitive band at 464 cm<sup>−1</sup>. The coordination equilibrium not only depends on the pH but is also affected by the buffer, the salt concentration, and the binding of the natural redox partner cytochrome <i>c</i><sub>552</sub>. These changes of the coordination equilibrium are attributed to the perturbation of the hydrogen bonding network at the catalytic center that is connected to the protein surface via a relay of hydrogen bonds. Environmental changes at the catalytic site are sensitively reflected by the formyl stretching of heme <i>a</i><sub>3</sub>. The unique structural properties of the <i>ba</i><sub>3</sub> oxidase may be related to the unusual proton pump efficiency and heme <i>a</i><sub>3</sub> redox potential. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: S53–S63, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 S5","pages":"S53-S63"},"PeriodicalIF":0.0,"publicationDate":"1999-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:5+<S53::AID-BSPY6>3.0.CO;2-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21374369","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 15
Partial intercalation with nucleic acids of peptides containing aromatic and basic amino acids 部分插入含有芳香和碱性氨基酸的多肽的核酸
Biospectroscopy Pub Date : 1999-09-22 DOI: 10.1002/(SICI)1520-6343(1999)5:5<313::AID-BSPY6>3.0.CO;2-G
Cynthia Robledo-Luiggi, Marisol Vera, Liliana Cobo, Ervia Jaime, Carmen Martínez, José L. González
{"title":"Partial intercalation with nucleic acids of peptides containing aromatic and basic amino acids","authors":"Cynthia Robledo-Luiggi,&nbsp;Marisol Vera,&nbsp;Liliana Cobo,&nbsp;Ervia Jaime,&nbsp;Carmen Martínez,&nbsp;José L. González","doi":"10.1002/(SICI)1520-6343(1999)5:5<313::AID-BSPY6>3.0.CO;2-G","DOIUrl":"10.1002/(SICI)1520-6343(1999)5:5<313::AID-BSPY6>3.0.CO;2-G","url":null,"abstract":"<p>A series of oligopeptides containing aromatic and basic residues were synthesized and their interactions with double-stranded nucleic acids studied by proton and phosphorus NMR, viscometry, and DNA melting temperature (<i>T</i><sub><i>m</i></sub>). The oligopeptides prepared contain two aromatic amino acids (phenylalanine or <i>p</i>-nitrophenylalanine) as well as one or two lysyl residues. The nucleic acids studied were calf thymus DNA, poly(dA-dT)<sub>2</sub>, poly(dA) · poly(dT), poly(dG-dC)<sub>2</sub>, poly(dG) · poly(dC), and d(ATGCAT)<sub>2</sub>. The results obtained show stacking of both aromatic residues of the oligopeptides with the nucleic acids. Higher upfield shifts of the aromatic amino acid residues were always observed with alternating nucleic acids and were higher with poly(dA-dT)<sub>2</sub> in all cases. Evidence for two types of complexes of Lys-Phe-Gly-Gly-<i>p</i>-NO<sub>2</sub>Phe-LysNH<sub>2</sub> with DNA was obtained by NMR, one attributed to a purely electrostatic complex and another involving stacking interactions. Studies with d(ATGCAT)<sub>2</sub> indicate that the aromatic residues of the oligopeptides were stacked with the terminal AT base pairs preferentially binding at the ends of the hexanucleotide. © 1999 John Wiley &amp; Sons, Inc. Biospectroscopy 5: 313–322, 1999</p>","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"5 5","pages":"313-322"},"PeriodicalIF":0.0,"publicationDate":"1999-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1999)5:5<313::AID-BSPY6>3.0.CO;2-G","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90635137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase 蛋白质环境对酵母细胞色素c过氧化物酶铁和铁配合物磁性圆二色性的影响
Biospectroscopy Pub Date : 1999-09-22 DOI: 10.1002/(SICI)1520-6343(1999)5:5+<S42::AID-BSPY5>3.0.CO;2-9
Alycen E. Pond, Masanori Sono, Elena A. Elenkova, David B. Goodin, Ann M. English, John H. Dawson
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引用次数: 10
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