Biospectroscopy最新文献_第6页

Spatially localized ballistic two-photon excitation in scattering media† 散射介质中空间定域弹道双光子激发†

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5<303::AID-BSPY2>3.0.CO;2-X

Henryk Szmacinski, Ignacy Gryczynski, Joseph R. Lakowicz

引用次数: 27

Resonance Raman spectroscopic study of the caa3 oxidase from Thermus thermophilus 嗜热热菌caa3氧化酶的共振拉曼光谱研究

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:6<365::AID-BSPY2>3.0.CO;2-C

S. Gerscher, P. Hildebrandt, T. Soulimane, G. Buse

{"title":"Resonance Raman spectroscopic study of the caa3 oxidase from Thermus thermophilus","authors":"S. Gerscher, P. Hildebrandt, T. Soulimane, G. Buse","doi":"10.1002/(SICI)1520-6343(1998)4:6<365::AID-BSPY2>3.0.CO;2-C","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:6<365::AID-BSPY2>3.0.CO;2-C","url":null,"abstract":"The terminal caa3 oxidase of Thermus thermophilus has been studied by resonance Raman spectroscopy. Using different excitation wavelengths in the Soret band region, it was possible to disentangle the resonance Raman spectra of the fully oxidized and fully reduced state in terms of the component spectra of the individual hemes a, a3, and c. For the heme a and a3 groups, the spectra reveal only minor differences compared to those of beef heart cytochrome c oxidase attributable to subtle modifications of the heme environment. These differences are not more pronounced than those between the oxidases from beef heart and Paracoccus denitrificans confirming the view that this oxidase of Th. thermophilus is a typical member of the aa3 oxidase superfamily. The heme c component spectra display far-reaching similarities with those of c-type cytochromes which serve as mobile electron carriers in the respiratory chain. These results imply that caa3 oxidase represents an integrated version of the noncovalent redox complex between cytochrome c and cytochrome c oxidase in higher organisms. On the other hand, the structural changes of cytochrome c in the noncovalent complex have no counterpart in the heme c component of the caa3 oxidase indicating a specific cytochrome c binding site for the mitochondrial enzyme. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 365–377, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 6","pages":"365-377"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:6<365::AID-BSPY2>3.0.CO;2-C","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85748271","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: 17

Understanding heme cavity structure of peroxidases: Comparison of electronic absorption and resonance Raman spectra with crystallographic results 了解过氧化物酶的血红素腔结构:电子吸收和共振拉曼光谱与晶体学结果的比较

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5+<S3::AID-BSPY2>3.0.CO;2-R

Giulietta Smulevich

引用次数: 48

Two-dimensional mid-IR and near-IR correlation spectra of ribonuclease A: Using overtones and combination modes to monitor changes in secondary structure 核糖核酸酶A的二维中红外和近红外相关光谱:利用泛音和组合模式监测二级结构的变化

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5+<S19::AID-BSPY3>3.0.CO;2-N

Christian P. Schultz, Heinz Fabian, Henry H. Mantsch

{"title":"Two-dimensional mid-IR and near-IR correlation spectra of ribonuclease A: Using overtones and combination modes to monitor changes in secondary structure","authors":"Christian P. Schultz, Heinz Fabian, Henry H. Mantsch","doi":"10.1002/(SICI)1520-6343(1998)4:5+<S19::AID-BSPY3>3.0.CO;2-N","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5+<S19::AID-BSPY3>3.0.CO;2-N","url":null,"abstract":"We introduce near-IR spectroscopy as an ancillary tool for monitoring structural changes of proteins in aqueous solution using ribonuclease A (RNase A) as a model protein. The thermal unfolding of RNase A results in clear spectral changes in the near-IR and the mid-IR regions. In the near-IR the most pronounced changes are observed in the spectral region between 4820 and 4940 cm−1. The strong NH combination band found at 4867 cm−1 in the spectrum of native RNase A shifts to 4878 cm−1 upon thermal unfolding. Hydrogen–deuterium exchange experiments that validate the NH character of this mode can also be used to estimate the number of unexchanged amide protons after exposure to D2O. The transition profiles and temperatures derived from the temperature dependence of the NH combination mode were found to be practically identical with those derived from the temperature dependence of the CO amide I band in the mid-IR region, demonstrating that the near-IR region can be used as a conformation-sensitive monitor for the thermally induced unfolding of proteins in H2O solution. A 2-dimensional correlation analysis was applied to the mid-IR and near-IR spectra of RNase A to establish correlations between IR bands in both regions. The correlation analysis demonstrates that the thermal unfolding of RNase A is not a completely cooperative process; rather it begins with some changes in β-sheet structure, followed by the loss of α-helical structures, and then ending with the unfolding of the remaining β-sheets. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S19–S29, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 S5","pages":"S19-S29"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5+<S19::AID-BSPY3>3.0.CO;2-N","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701168","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: 47

13C- and 57Fe-NMR studies of the FeCO unit of heme proteins and synthetic model compounds in solution: Comparison with IR vibrational frequencies and X-ray structural data 血红素蛋白和合成模型化合物的Fe- C- O单元的13C-和57Fe-NMR研究:与红外振动频率和x射线结构数据的比较

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5+<S57::AID-BSPY7>3.0.CO;2-1

Charalampos G. Kalodimos, Ioannis P. Gerothanassis, Geoffrey E. Hawkes

{"title":"13C- and 57Fe-NMR studies of the FeCO unit of heme proteins and synthetic model compounds in solution: Comparison with IR vibrational frequencies and X-ray structural data","authors":"Charalampos G. Kalodimos, Ioannis P. Gerothanassis, Geoffrey E. Hawkes","doi":"10.1002/(SICI)1520-6343(1998)4:5+<S57::AID-BSPY7>3.0.CO;2-1","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5+<S57::AID-BSPY7>3.0.CO;2-1","url":null,"abstract":"13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm when several hemoglobin CO and myoglobin CO species at different pHs are included. Both heme models and heme proteins obey a similar excellent linear δ(13C) versus ν(CO) relationship that is primarily due to modulation of π backbonding from Fe dπ to the CO π* orbital by the distal pocket polar interactions. There is no direct correlation between δ(13C) and FeCO geometry. The poor monotonic relation between δ(13C) and ν(FeC) indicates that the iron-carbon π bonding is not a primary factor influencing δ(13C) and δ(57Fe). The δ(57Fe) was found to be extremely sensitive to deformation of the porphyrin geometry, and increased shielding by more than 600 ppm with increased ruffling was observed for various heme models of known X-ray structures. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S57–S69, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 S5","pages":"S57-S69"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5+<S57::AID-BSPY7>3.0.CO;2-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701093","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: 3

Molecular dynamics simulations of biomembrane models 生物膜模型的分子动力学模拟

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5+<S41::AID-BSPY5>3.0.CO;2-G

G. Vergoten

引用次数: 0

Composition, constitution, and interaction of bone with hydroxyapatite coatings determined by FT Raman microscopy 用FT拉曼显微镜测定骨与羟基磷灰石涂层的组成、构成和相互作用

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:6<403::AID-BSPY5>3.0.CO;2-M

Bernd Dippel, Reinhold T. Mueller, Andreas Pingsmann, Bernhard Schrader

{"title":"Composition, constitution, and interaction of bone with hydroxyapatite coatings determined by FT Raman microscopy","authors":"Bernd Dippel, Reinhold T. Mueller, Andreas Pingsmann, Bernhard Schrader","doi":"10.1002/(SICI)1520-6343(1998)4:6<403::AID-BSPY5>3.0.CO;2-M","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:6<403::AID-BSPY5>3.0.CO;2-M","url":null,"abstract":"An optimized FT Raman microscope (inverted microscope with high throughput of radiation) was developed that allows minimal sample preparation and Raman spectroscopy without fluorescence. A quantitative determination of the mineralization of bone tissue and hydroxyapatite (HA) coatings of hip and knee prostheses was performed. The lateral resolution reached down to 10 μm. The distribution of the HA content in the coatings investigated was found to be similar all the time. This result was independent of the composition of the coatings and the history of the whole prosthesis. In the immediate vicinity of the prosthesis a large HA content could be observed that decreased to a minimum towards the periphery of the coating and increased at the site of the ongrown bone. For the interface between bone and HA coating a transitional zone was observed at a lateral distance of 30–40 μm to the implant. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 403–412, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 6","pages":"403-412"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:6<403::AID-BSPY5>3.0.CO;2-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20760942","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: 19

Characterization of island films as surface-enhanced Raman spectroscopy substrates for detecting low antitumor drug concentrations at single cell level 岛膜作为表面增强拉曼光谱底物在单细胞水平检测低抗肿瘤药物浓度的表征

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5+<S71::AID-BSPY8>3.0.CO;2-Z

G. D. Sockalingum, A. Beljebbar, H. Morjani, J. F. Angiboust, M. Manfait

{"title":"Characterization of island films as surface-enhanced Raman spectroscopy substrates for detecting low antitumor drug concentrations at single cell level","authors":"G. D. Sockalingum, A. Beljebbar, H. Morjani, J. F. Angiboust, M. Manfait","doi":"10.1002/(SICI)1520-6343(1998)4:5+<S71::AID-BSPY8>3.0.CO;2-Z","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5+<S71::AID-BSPY8>3.0.CO;2-Z","url":null,"abstract":"Gold and silver vacuum-deposited island films were characterized by studying deposition variables such as film thickness, evaporation rate, and substrate temperature. For both metals, these parameters were correlated with the surface-enhanced Raman spectroscopy (SERS) effect and an increase in film thickness and low evaporation rates were shown to upshift the wavelength at maximum optical density (λmax) and increase the optical density of the substrates. In contrast, pre- and postdeposition annealing of gold films led to the formation of substrates that exhibited a downshift of λmax. Our spectral data also indicated that silver films are substrates that are more suited for SERS applications where high frequency visible excitations are used. Measurements on gold films classified them into two groups: thin Au films (10–50 Å) well adapted for red excitations and thicker ones that are operative in the near infrared. SERS results, which were obtained from a single HL60 cell treated with micromolar drug quantities, placed on thin gold island films indicated that these island films could be future promising substrates for SERS imaging at the cellular level. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S71–S78, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 S5","pages":"S71-S78"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5+<S71::AID-BSPY8>3.0.CO;2-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20701094","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

Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata 果胶Lucina pectinata硫化氢结合血红蛋白I中血红素乙烯基的取向

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5<311::AID-BSPY3>3.0.CO;2-T

Eilyn Silfa, Maritza Almeida, Jose Cerda, Shaoxiong Wu, Juan López-Garriga

{"title":"Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata","authors":"Eilyn Silfa, Maritza Almeida, Jose Cerda, Shaoxiong Wu, Juan López-Garriga","doi":"10.1002/(SICI)1520-6343(1998)4:5<311::AID-BSPY3>3.0.CO;2-T","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5<311::AID-BSPY3>3.0.CO;2-T","url":null,"abstract":"Hemoglobin I (HbI) from the claim Lucina pectinata is a unique heme protein that binds and transfers hydrogen sulfide (H2S) to a symbiotic bacteria. The metcyano, metaquo, carbon monoxy, oxy, and deoxy complexes of HbI were studied by resonance Raman (RR) spectroscopy, and the metcyano and carbon monoxy complexes were also studied by 1H-NMR. The results indicate a unique orientation of the heme 2-vinyl group relative to other heme proteins. The RR spectra of the HbICO, metHbICN, metHbIH2O, HbIO2 and deoxyHbI heme derivatives show a band at 1621 cm−1 and a shoulder at 1626 cm−1, indicative of an out-of-plane position for one of the vinyls relative to the other one. Spin-lattice relaxation properties of protons in the metHbICN complex also suggest a unique orientation for the heme 2-vinyl group of HbI. The longitudinal relaxation time (T1) for the 2-Hα, 2-Hβc, and Hβt protons are 120 ms, 115 ms, and 135 ms, respectively. The data from both techniques suggest an out-of-plane and trans-oriented 2-vinyl group, and an in-plane and cis-oriented 4-vinyl group for the low-spin complexes of HbI. These results imply that the electron withdrawing character of the out-of-plane vinyl group contributes to the stability of the heme Fe+3 oxidation state, facilitates the binding of the H2S ligand, and promotes the stability of this ferric H2S complex. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 311–326, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 5","pages":"311-326"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5<311::AID-BSPY3>3.0.CO;2-T","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20700617","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

Fluorescence and surface-enhanced Raman study of 9-aminoacridine in relation to its aggregation and excimer emission in aqueous solution and on silver surface 9-氨基吖啶在水溶液和银表面的聚集和准分子发射的荧光和表面增强拉曼研究

Biospectroscopy Pub Date : 1999-01-06 DOI: 10.1002/(SICI)1520-6343(1998)4:5<327::AID-BSPY4>3.0.CO;2-H

A. Murza, S. Sánchez-Cortés, J. V. García-Ramos

{"title":"Fluorescence and surface-enhanced Raman study of 9-aminoacridine in relation to its aggregation and excimer emission in aqueous solution and on silver surface","authors":"A. Murza, S. Sánchez-Cortés, J. V. García-Ramos","doi":"10.1002/(SICI)1520-6343(1998)4:5<327::AID-BSPY4>3.0.CO;2-H","DOIUrl":"10.1002/(SICI)1520-6343(1998)4:5<327::AID-BSPY4>3.0.CO;2-H","url":null,"abstract":"Fluorescence spectroscopy and surface-enhanced Raman spectroscopy (SERS) have been applied to study the aggregation and excimer emission of 9-aminoacridine (9AA) and 9-aminoacridine hydrochloride (9AA-HCl) in aqueous solution and on silver colloids. The effect of the drug concentration, pH, and chloride concentration on these processes has been investigated. The excimer emission of 9AA is connected to the dimerization of this drug in solution: the formation of 9AA dimers is greatly favored when the drug is under the amino form at neutral and acidic pH, while at alkaline pH the imino 9AA form tends to form large-sized aggregates which cannot be excited to render excimer emission. 9AA is adsorbed on the silver surface under two different forms: strongly and weakly attached 9AA, each one corresponding to the different drug tautomers: imino and amino. The interaction of 9AA with silver induces a charge transfer from the adsorbate to the metal leading to a remarkable fluorescence quenching, a basicity decrease of the adsorbed drug and a considerable weakening of the dimer-excimer emission. Furthermore, an attribution of the main Raman features appearing in the SERS spectra has been proposed, providing marker bands for the imino and amino 9AA tautomers, and a mechanism for the molecular dimerization is also suggested. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 327–339, 1998","PeriodicalId":9037,"journal":{"name":"Biospectroscopy","volume":"4 5","pages":"327-339"},"PeriodicalIF":0.0,"publicationDate":"1999-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/(SICI)1520-6343(1998)4:5<327::AID-BSPY4>3.0.CO;2-H","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20700619","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: 28