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排序方式: 共有100条查询结果,搜索用时 15 毫秒
1.
Summary Four derivatives ofCarcinus maenas hemocyanin containing Co(II) in the active site have been prepared under different experimental conditions. Two of them contain one Co(II) ion/active site and most probably represent isomeric forms containing Co(II) either in the fast-reacting or in the slow-reacting position within the active site. A third derivative contains two Co(II) ions active site, which reproduces the metal/protein stoichiometry of native hemocyanin. The fourth derivative is a metal hybrid form containing one Cu(I) ion and one Co(II) ion/active site. The derivatives have been characterized by absorption, circular dichroic and fluorescence spectroscopies. The results indicate that in all derivatives the metal is bound with a low coordination number, in agreement with the presence of three histidine residues/copper ion in the native protein. The two alternative metal-binding positions have different structures as shown by the different spectroscopic properties of the bound Co(II) ions. A marked hyperchromic effect on the optical absorption of Co(II) is observed as a result of the presence of a metal ion in the neighbouring metal-binding position in the active site. 相似文献
2.
Spectroscopic studies on Neurospora copper metallothionein 总被引:1,自引:0,他引:1
The spectral properties of Neurospora copper metallothionein were investigated and compared with those of the Cu(I)-2-mercaptoethanesulfonic acid complex. In both cases, the absorption spectra are rather similar, showing a characteristic shoulder at approximately 250 nm. However, marked differences were observed in their emissive properties. Thus, only metallothionein emits detectable luminescence in solution, but both the copper protein and the Cu(I) complex are luminescent at 77 K. The circular dichroism spectrum of Neurospora copper metallothionein shows several Cotton extrema attributable to asymmetry in metal coordination. The influence of HgCl2 and p-(chloromercuri)benzoate on the spectral properties of metallothionein was also investigated. The two mercurials exerted a pronounced effect on the electronic absorption, chiroptical, and emissive properties of the protein. Spectroscopic titrations followed by gel filtration experiments indicate that two mercurials can be bound per metallothionein molecule without loss of copper. This binding is responsible for the disappearance of the emissive properties of metallothionein and for the distinct changes in its electronic absorption and circular dichroism spectra. From these data, it is suggested that the Cu(I) ions are coordinated to the cysteinyl residues in the form of a single metal cluster. 相似文献
3.
M Beltramini L Bubacco B Salvato L Casella M Gullotti S Garofani 《Biochimica et biophysica acta》1992,1120(1):24-32
The binding of various ligand molecules to the binuclear Cu(I) site of deoxy-hemocyanin has been investigated through the changes produced in the aromatic region of the circular dichroism spectrum of the protein, where a cluster of tryptophan residues located in the vicinity of copper site undergo conformational reorientations in the presence of exogenous ligands coordinated to the metal. In agreement with expectations, the binuclear site of arthropod hemocyanin is severely hindered to the access of exogenous ligands except for very small molecules like CO, O2 or CN- while for mollusc proteins ligands such as thiourea and 2-mercaptoethanol bind easily to the Cu(I) sites. However, the access of the ligand becomes progressively hindered and eventually prevented as the size of substituents on the ligand increases. 相似文献
4.
Mazzini A Beltramini M Favilla R Cavatorta P Di Muro P Salvato B 《Biophysical chemistry》1994,52(2):145-156
The interaction of 4',6-diamidino-2-phenylindole (DAPI) with Carcinus maenas hemocyanin has been investigated by steady state fluorescence, dynamic fluorescence and circular dichroism measurements. The dye binds to apohemocyanin (without copper) as well as to oxygenated hemocyanin and to deoxygenated hemocyanin with very similar affinities (kd approximately equal to 1 microM ) and number of binding sites (one per subunit). In contrast, the fluorescence quantum yield enhancement of DAPI bound to oxygenated hemocyanin is nearly 60% lower than that observed for deoxygenated and apo forms. The decrease of fluorescence of the dye bound to deoxygenated hemocyanin is a sigmoidal function of the oxygen partial pressure, specular to that observed by following the absorbance of the copper-oxygen charge transfer band at 340 nm. This result provides preliminary evidence that DAPI may be used as a functional probe to monitor the cooperative binding of oxygen to the protein. The higher fluorescence quantum yield of DAPI bound to either apohemocyanin or deoxygenated protein is characterized by a single fluorescence decay with lifetime of about 3 ns, while with the oxygenated protein two components of about 1 ns and 3.0 ns are observed. This result is interpreted assuming the existence of two rotamers of DAPI in solution (Szabo et al. Photochem. Photobiol. 44 (1986) 143-150) both able to interact with oxygenated hemocyanin but only one to deoxygenated and apo forms. We conclude that the different fluorescence behaviour of the dye induced by the presence of oxygen bound to the protein is probably due to a structural change of hemocyanin in cooperative interaction with oxygen. Furthermore, the interaction is confirmed by the induced negative ellipticity of DAPI bound to apohemocyanin and deoxy-hemocyanin and by the increase of fluorescence anisotropy of DAPI bound to all forms of protein investigated. 相似文献
5.
Eugenio Vitrano Antonio Cupane Maurizio Leone Valeria Militello Lorenzo Cordone Benedetto Salvato Mariano Beltramini Luigi Bubacco Gian Paolo Rocco 《European biophysics journal : EBJ》1993,22(3):157-167
In this work we report the optical absorption spectra of three cobalt-substituted derivatives of hemocyanin (He) from Carcinus maenas, in the temperature range 300–20 K. The derivatives studied are the mononuclear (Co2+)-He with a single cobalt ion in the CuA site, the binuclear (Co2+)2-He and the binuclear mixed metal (Co2+-Cu1+)-He. At low temperature three main bands are clearly resolved; the temperature dependence of their zeroth, first and second moments sheds light on the stereodynamic properties in the surroundings of the chromophore. Within the limits of the reported analysis, in the binuclear derivatives the motions coupled to the chromophore appear to be essentially harmonic in the whole temperature range investigated; moreover the data are consistent with the presence of an exogenous ligand strongly bound to the two metal ions. For the mononuclear derivative an essentially harmonic behavior is evident only up to 200 K where the data are consistent with the presence of an exogenous ligand much less strongly bound, while at higher temperatures the behavior of the spectra indicates the onset of very large anharmonic contributions to motions, that plausibly involve the above exogenous ligand and, quite likely, the entire active site.Abbreviations He
Hemocyanin
- M0
zeroth moment
- M1
first moment
- M2
second moment
- (Co2–)2-He
binuclear bicobalt hemocyanin derivative
- (Co2+)-He
mononuclear monocobalt hemocyanin derivative
- (Co2+-Cu1+)-He
binuclear mixed metals hemocyanin derivative
- LFT
ligand field theory
- CT
charge transfer
- EPR
electronic paramagnetic resonance
- XANES
X-ray absorption near edge structure
Correspondence to: L. Cordone 相似文献
6.
Fernanda A. H. Batista Leandro S. Goto Wanius Garcia Derminda I. de Moraes Mario de Oliveira Neto Igor Polikarpov Marcia R. Cominetti Heloísa S. Selistre-de-Araújo Leila M. Beltramini Ana Paula Ulian Araújo 《European biophysics journal : EBJ》2010,39(8):1193-1205
Lectins have been classified into a structurally diverse group of proteins that bind carbohydrates and glycoconjugates with
high specificity. They are extremely useful molecules in the characterization of saccharides, as drug delivery mediators,
and even as cellular surface makers. In this study, we present camptosemin, a new lectin from Camptosema ellipticum. It was characterized as an N-acetyl-d-galactosamine-binding homo-tetrameric lectin, with a molecular weight around 26 kDa/monomers. The monomers were stable over
a wide range of pH values and exhibited pH-dependent oligomerization. Camptosemin promoted adhesion of breast cancer cells
and hemagglutination, and both activities were inhibited by its binding of sugar. The stability and unfolding/folding behavior
of this lectin was characterized using fluorescence and far-UV circular dichroism spectroscopies. The results indicate that
chemical unfolding of camptosemin proceeds as a two-state monomer-tetramer process. In addition, small-angle X-ray scattering
shows that camptosemin behaves as a soluble and stable homo-tetramer molecule in solution. 相似文献
7.
Hemocyanins from Crustacea usually are found as 1 × 6 or 2 × 6-meric assemblies. An exception is the hemocyanin isolated from thalassinidean shrimps where the main component is a 24-meric structure. Our analysis of oxygen binding data of the thalassinidean shrimp Upogebia pusilla based on a three-state MWC-model revealed that despite the 24-meric structure the functional properties can be described very well based on the hexamer as allosteric unit. In contrast to the hemocyanins from other thalassinidean shrimps the oxygen affinity of hemocyanin from U. pusilla is increased upon addition of l-lactate. A particular feature of this hemocyanin seems to be that l-lactate already enhances oxygen affinity under resting conditions which possibly compensates the rather low intrinsic affinity observed in absence of l-lactate. The fast rate of oxygen dissociation might indicate that in this hemocyanin a higher cooperativity is less important than a fast response of saturation level to changes in oxygen concentration. 相似文献
8.
The structural properties of the hemocyanin isolated from the Mediterranean mud shrimp, Upogebia pusilla (Decapoda: Thalassinidea), were investigated. Our intent was to make use of the U. pusilla case to perform a structural comparison between crustacean and chelicerate 4x6-meric hemocyanins. The thalassinidean hemocyanin appears similar in size but different in structural organization compared to the chelicerate 4x6-mer. Ultracentrifuge analyses on the purified protein revealed a sedimentation coefficient of 39S, typical of 4x6 hemocyanins. Electron micrographs are in agreement with a model in which four 2x6-meric building blocks are arranged in a tetrahedron-like quaternary structure and not in the quasi-square-planar orientation characteristic of the chelicerate protein. Size-exclusion chromatography-fast protein chromatography analysis showed elevated instability of the protein in absence of divalent ions or at pH values higher than 8.0. This analysis also shows that the dissociation of the U. pusilla 4x6-meric hemocyanin into hexamers occurs without any intermediate 2x6-meric state, in contrast with the dissociation profile of the chelicerate protein exhibiting several dissociation intermediates. The oxygen-binding properties of U. pusilla hemocyanin were studied to disclose possible effects by the typical allosteric effectors that modulate the functional properties of crustacean hemocyanin. A marked Bohr and lactate effect, but no significant influence of urate, on the oxygen affinity of U. pusilla hemocyanin were found. 相似文献
9.
Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles 总被引:1,自引:0,他引:1
Campana PT Beltramini LM Costa-Filho AJ Tonarelli G Lottersberger J Bianconi ML 《Biophysical chemistry》2005,113(2):175-182
We studied the interaction of the peptide AAMQMLKETINEEAAEWDRVHPVHAGPIA from the HIV-1 p24 protein in the presence of SDS (anionic) and CTABr (cationic) micelles at pH 7.0 by circular dichroism, fluorescence, and electron spin resonance (ESR). The micelles induced secondary structure as well as a blue shift in the tryptophan fluorescence emission, indicating an interaction between the peptide and the micelles. However, different contents of secondary structure elements were found when the peptide interacts with SDS or CTABr micelles. Steady-state anisotropy indicates a constraint on the rotational mobility of the tryptophan residue of the peptide upon interaction with micelles. ESR studies pointed to different locations for the peptide in either micelle. Our results suggested that at least part of the peptide might be located at the hydrophobic core of the CTABr micelles, probably at the C-terminal region, while it is more inserted into the SDS micelles. 相似文献
10.
Beltramini M Colangelo N Giomi F Bubacco L Di Muro P Hellmann N Jaenicke E Decker H 《The FEBS journal》2005,272(8):2060-2075
The hemocyanin of the tiger shrimp, Penaeus monodon, was investigated with respect to stability and oxygen binding. While hexamers occur as a major component, dodecamers and traces of higher aggregates are also found. Both the hexamers and dodecamers were found to be extremely stable against dissociation at high pH, independently of the presence of calcium ions, in contrast to the known crustacean hemocyanins. This could be caused by only a few additional noncovalent interactions between amino acids located at the subunit-subunit interfaces. Based on X-ray structures and sequence alignments of related hemocyanins, the particular amino acids are identified. At all pH values, the p50 and Bohr coefficients of the hexamers are twice as high as those of dodecamers. While the oxygen binding of hexamers from crustaceans can normally be described by a simple two-state model, an additional conformational state is needed to describe the oxygen-binding behaviour of Penaeus monodon hemocyanin within the pH range of 7.0 to 8.5. The dodecamers bind oxygen according to the nested Monod-Whyman-Changeaux (MWC) model, as observed for the same aggregation states of other hemocyanins. The oxygen-binding properties of both the hexameric and dodecameric hemocyanins guarantee an efficient supply of the animal with oxygen, with respect to the ratio between their concentrations. It seems that under normoxic conditions, hexamers play the major role. Under hypoxic conditions, the hexamers are expected not to be completely loaded with oxygen. Here, the dodecamers are supposed to be responsible for the oxygen supply. 相似文献