Biospectroscopy最新文献_第9页

Spectrophotometry of human hemoglobin in the midinfrared region 中红外区人血红蛋白的分光光度法

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1997)3:3<225::AID-BSPY6>3.0.CO;2-4

J. Todd Kuenstner, Karl Norris, Victor F. Kalasinsky

引用次数: 16

Effect of surface modifiers on the electrode reactions and conformation of cytochrome c3 adsorbed on a silver electrode 表面改性剂对细胞色素c3在银电极上吸附的电极反应和构象的影响

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1998)4:3<161::AID-BSPY2>3.0.CO;2-7

Daisuke Hobara, Katsumi Niki, Therese M. Cotton

{"title":"Effect of surface modifiers on the electrode reactions and conformation of cytochrome c3 adsorbed on a silver electrode","authors":"Daisuke Hobara, Katsumi Niki, Therese M. Cotton","doi":"10.1002/(SICI)1520-6343(1998)4:3<161::AID-BSPY2>3.0.CO;2-7","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:3<161::AID-BSPY2>3.0.CO;2-7","url":null,"abstract":"Surface-enhanced resonance Raman scattering and electroreflectance voltammetry were used to investigate the effect of electrode surface modification on the structure and redox properties of cytochrome c3 immobilized on Ag surfaces. It is shown that the redox reactions of cytochrome c3 are more reversible at an 11-mercaptoundecanoic acid modified Ag electrode as compared to a bare metal surface. The heme of cytochrome c3 is in a mixed low and high spin state when adsorbed at the bare electrode, whereas only the low spin form is present on the 11-mercaptoundecanoic acid modified electrode, suggesting that the native conformation is maintained in the latter case. The reduction potential is close to that of the most positive macroscopic potential as determined by electroreflectance spectroscopy. In contrast, the reduction potential as determined by SERRS undergoes a large positive shift in the presence of 4,4′-bipyridine, the magnitude of which is dependent upon the concentration of 4,4′-bipyridine. These results indicate that the effect of the cytochrome c3 interaction with the 4,4′-bipyridine-modified surface is significantly different as compared to its interaction with the 11-mercaptoundecaodoic acid modified surface. Moreover, the results emphasize that electrode modifiers can have dramatically different effects on the redox properties of different proteins. It is well known that 4,4′-bipyridine acts as a redox promoter in the case of cytochrome c, whereas no electrochemical or electroreflectance response was observed in the case of cytochrome c3. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 161–170, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 3","pages":"161-170"},"PeriodicalIF":0.0,"publicationDate":"1998-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:3<161::AID-BSPY2>3.0.CO;2-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90644032","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: 14

Oxazole yellow dye interactions with short DNA oligomers of homogeneous base composition and their hybrids 恶唑黄染料与均匀碱基组成的短DNA低聚物及其杂种的相互作用

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1998)4:1<17::AID-BSPY2>3.0.CO;2-P

Lara D. Simon, Kimberly H. Abramo, Jarrett K. Sell, Linda B. McGown

{"title":"Oxazole yellow dye interactions with short DNA oligomers of homogeneous base composition and their hybrids","authors":"Lara D. Simon, Kimberly H. Abramo, Jarrett K. Sell, Linda B. McGown","doi":"10.1002/(SICI)1520-6343(1998)4:1<17::AID-BSPY2>3.0.CO;2-P","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:1<17::AID-BSPY2>3.0.CO;2-P","url":null,"abstract":"Interactions between short single-stranded DNA oligomers of homogeneous base composition and the fluorescent probes oxazole yellow (YO) and its homodimer YOYO are described. The oligomers included 15-mers and 30-mers of polydA, polydT, polydG, and polydC. Interactions between the dyes and DNA hybrids formed from complementary homogeneous strands of equal length were also investigated. No interactions were observed between the dyes and the monomeric monophosphate nucleosides A, G, T, or C. The dyes were found to interact much more strongly with the purine oligomers polydA and polydG than with the pyrimidine oligomers polydT and polydC. PolydA of both lengths has strong interactions with YOYO, whereas the polydG 30-mer interacts strongly with monomeric YO. The 15-mers of polydG and polydC of both lengths show little interaction with either dye. Interactions of the dyes with the polydA/polydT and polydG/polydC hybrids tend to be dominated by interactions with polydA and polydG, respectively. Although dye interactions generally were facilitated by hybridization, particularly for polydA/polydT, the interactions were similar to those with the single strands and different from those that have been observed in long double-stranded DNA. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 17–25, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 1","pages":"17-25"},"PeriodicalIF":0.0,"publicationDate":"1998-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:1<17::AID-BSPY2>3.0.CO;2-P","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20469935","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

Raman scattering tensors of tyrosine 酪氨酸的拉曼散射张量

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1998)4:1<61::AID-BSPY7>3.0.CO;2-V

Masamichi Tsuboi, Yoshiko Ezaki, Misako Aida, Mika Suzuki, Abliz Yimit, Koichi Ushizawa, Toyotoshi Ueda

{"title":"Raman scattering tensors of tyrosine","authors":"Masamichi Tsuboi, Yoshiko Ezaki, Misako Aida, Mika Suzuki, Abliz Yimit, Koichi Ushizawa, Toyotoshi Ueda","doi":"10.1002/(SICI)1520-6343(1998)4:1<61::AID-BSPY7>3.0.CO;2-V","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:1<61::AID-BSPY7>3.0.CO;2-V","url":null,"abstract":"Polarized Raman scattering measurements have been made of a single crystal of L-tyrosine by the use of a Raman microscope with the 488.0-nm exciting beam from an argon ion laser. The L-tyrosine crystal belongs to the space group P212121 (orthorhombic), and Raman scattering intensities corresponding to the aa, bb, cc, ab and ac components of the crystal Raman tensor have been determined for each prominent Raman band. A similar set of measurements has been made of L-tyrosine-d4, in which four hydrogen atoms on the benzene ring are replaced by deuterium atoms. The effects of NH3 → ND3 and OH → OD on the Raman spectrum have also been examined. In addition, depolarization ratios of some bands of L-tyrosine in aqueous solutions of pH 13 and pH 1 were examined. For comparison with these experimental results, on the other hand, ab initio molecular orbital calculations have been made of the normal modes of vibration and their associated polarizability oscillations of the L-tyrosine molecule. On the basis of these experimental data and by referring to the results of the calculations, discussions have been presented on the Raman tensors associated to some Raman bands, including those at 829 cm−1 (benzene ring breathing), 642 cm−1 (benzene ring deformation), and 432 cm−1 (Cα-Cβ-Cγ bending). © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 61–71, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 1","pages":"61-71"},"PeriodicalIF":0.0,"publicationDate":"1998-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:1<61::AID-BSPY7>3.0.CO;2-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20470395","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: 44

Amphotericin B toxicity as related to the formation of oxidatively modified low-density lipoproteins 两性霉素B毒性与氧化修饰低密度脂蛋白的形成有关

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1998)4:2<135::AID-BSPY6>3.0.CO;2-4

Joanna Barwicz, Isabelle Dumont, Claire Ouellet, Ilona Gruda

引用次数: 25

FT-Raman investigation of alkaloids in the liana Ancistrocladus heyneanus 山藤本植物生物碱的FT-Raman研究

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1998)4:2<113::AID-BSPY4>3.0.CO;2-6

E. Urlaub, J. Popp, W. Kiefer, G. Bringmann, D. Koppler, H. Schneider, U. Zimmermann, B. Schrader

引用次数: 33

A spectroscopic study of pigment gallstones in China 中国胆结石色素的光谱研究

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1997)3:5<371::AID-BSPY4>3.0.CO;2-5

X.-S. Zhou, G.-R. Shen, J.-G. Wu, W.-H. Li, Y.-Z. Xu, S.-F. Weng, R. D. Soloway, X.-B. Fu, W. Tian, Z. Xu, T. Shen, G.-X. Xu, E. Wentrup-Byrne

引用次数: 37

Periodic and chaotic precipitation phenomena in bile salt system related to gallstone formation 胆盐系统中与胆结石形成有关的周期性和混沌沉淀现象

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1997)3:3<195::AID-BSPY3>3.0.CO;2-5

Q. Peng, J.-G. Wu, R. D. Soloway, T.-D. Hu, W.-D. Huang, Y.-Z. Xu, L.-B. Wang, X.-F. Li, W.-H. Li, D.-F. Xu, G.-X. Xu

引用次数: 16

Femtosecond time-resolved spectroscopy of the primary photochemistry of phytochrome 光敏色素初级光化学的飞秒时间分辨光谱

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1997)3:6<421::AID-BSPY1>3.0.CO;2-3

Frank Andel III, K. C. Hasson, Feng Gai, Philip A. Anfinrud, Richard A. Mathies

{"title":"Femtosecond time-resolved spectroscopy of the primary photochemistry of phytochrome","authors":"Frank Andel III, K. C. Hasson, Feng Gai, Philip A. Anfinrud, Richard A. Mathies","doi":"10.1002/(SICI)1520-6343(1997)3:6<421::AID-BSPY1>3.0.CO;2-3","DOIUrl":"10.1002/(SICI)1520-6343(1997)3:6<421::AID-BSPY1>3.0.CO;2-3","url":null,"abstract":"Time-resolved absorption spectra of Pr phytochrome were obtained using a regeneratively amplified femtosecond titanium : sapphire laser system. The early time transient absorption spectra are comprised of prompt Pr photobleaching, stimulated emission, and excited-state absorption features that decay with a 24 ps time constant that matches the ground state appearance time of the primary photoproduct. Based on the 5 ns radiative lifetime calculated from the absorption and spontaneous emission spectra and the fluorescence quantum yield of 5.5 (± 0.5) × 10−3, we calculate an excited-state lifetime of 28 ps that agrees well with the directly determined lifetime. The transient absorption spectra are consistent with a primary photochemical reaction quantum yield of 0.15, and the absorption spectrum of the primary photoproduct closely resembles that of the low-temperature trapped intermediate, lumi-R. We conclude that the primary photoisomerization, which is believed to be a Z,syn → E,syn isomerization of the C15=C16 chromophore bond, occurs in 24 ps. © 1997 John Wiley & Sons, Inc. Biospectroscopy 3: 421–433, 1997","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"3 6","pages":"421-433"},"PeriodicalIF":0.0,"publicationDate":"1998-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1997)3:6<421::AID-BSPY1>3.0.CO;2-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83308239","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: 40

Distinction of the two binding sites of serum transferrin by resonance Raman spectroscopy 共振拉曼光谱法区分血清转铁蛋白的两个结合位点

Biospectroscopy Pub Date : 1998-12-07 DOI: 10.1002/(SICI)1520-6343(1997)3:6<435::AID-BSPY2>3.0.CO;2-%23

Sandra L. Mecklenburg, Anne B. Mason, Robert C. Woodworth, Robert J. Donohoe

{"title":"Distinction of the two binding sites of serum transferrin by resonance Raman spectroscopy","authors":"Sandra L. Mecklenburg, Anne B. Mason, Robert C. Woodworth, Robert J. Donohoe","doi":"10.1002/(SICI)1520-6343(1997)3:6<435::AID-BSPY2>3.0.CO;2-%23","DOIUrl":"https://doi.org/10.1002/(SICI)1520-6343(1997)3:6<435::AID-BSPY2>3.0.CO;2-%23","url":null,"abstract":"The resonance Raman (RR) data for a variety of transferrin samples were investigated to explore differences between the two active sites. The excitation wavelength dependence of the RR data in the low energy shift region (<900 cm−1) for diferric transferrin (Fe2Tf) reveals extensive changes in the relative intensities for some of the peaks, indicating that the visible and near ultraviolet absorption of the Fe2Tf protein is composed of several distinct transitions. The identity of the low-energy vibrations was explored by comparison of the data from Fe2Tf, two different binding site mutants of the N-terminal site half transferrin molecule, Tf/2N, and Fe2Tf in which the normal binding site carbonate was replaced with C18O32−. The higher energy RR spectra of the various samples are quite similar, whereas the low-energy band patterns are strongly influenced by the mutations and isotopic substitution. Comparison of the RR data obtained from Fe2Tf, Tf/2N, and C-terminal monoferric transferrin reveals that the intensities and energies of the modes below 900 cm−1 are different for the two binding sites. This result helps reveal an isolated electronic transition for the N-terminal active site near 365 nm, where laser excitation yields selective enhancement of the low-energy N-terminal modes. © 1997 John Wiley & Sons, Inc. Biospectroscopy 3: 435–444, 1997","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"3 6","pages":"435-444"},"PeriodicalIF":0.0,"publicationDate":"1998-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137649241","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