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1.
Braz J Microbiol ; 54(4): 2807-2815, 2023 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-37801221

RESUMO

The rate of infectious diseases started to be one of the major mortality agents in the healthcare sector. Exposed to increased bacterial infection by antibiotic-resistant bacteria became one of the complications that occurred for bone marrow transplant patients. Nanotechnology may provide clinicians and patients with the key to overcoming multidrug-resistant bacteria. Therefore, this study was conducted to clarify the prevalence of MDR bacteria in bone marrow transplant recipients and the use of Ag2O/ZnO nanocomposites to treat participants of diarrhea brought on by MDR bacteria following bone marrow transplantation (BMT). Present results show that pathogenic bacteria were present in 100 of 195 stool samples from individuals who had diarrhea. Phenotypic, biochemical, and molecular analysis clarify that Proteus mirabilis and Salmonella typhi were detected in 21 and 25 samples, respectively. Successful synthesis of Ag2O/ZnO nanocomposites with a particle enables to inhibition of both pathogens. The maximum inhibitory impact was seen on Salmonella typhi. At low doses (10-5 g/l), it prevented the growth by 53.4%, while at higher concentrations (10-1 g/l), Salmonella typhi was inhibited by 95.5%. Regarding Proteus mirabilis, at (10-5 g/l) Ag2O/ZnO, it was inhabited by 78.7%, but at higher concentrations (10-1 g/l), it was inhibited the growth by 94.6%. Ag2O/ZnO nanocomposite was therefore found to be the most effective therapy for MDR-isolated bacteria and offered promise for the treatment of MDR bacterial infections that cause diarrhea.


Assuntos
Proteus mirabilis , Óxido de Zinco , Humanos , Salmonella typhi , Óxido de Zinco/farmacologia , Óxido de Zinco/química , Medula Óssea , Transplante de Medula Óssea , Antibacterianos/farmacologia , Antibacterianos/química , Bactérias , Diarreia
2.
Commun Biol ; 4(1): 304, 2021 03 08.
Artigo em Inglês | MEDLINE | ID: mdl-33686186

RESUMO

A high-resolution structure of trimeric cyanobacterial Photosystem I (PSI) from Thermosynechococcus elongatus was reported as the first atomic model of PSI almost 20 years ago. However, the monomeric PSI structure has not yet been reported despite long-standing interest in its structure and extensive spectroscopic characterization of the loss of red chlorophylls upon monomerization. Here, we describe the structure of monomeric PSI from Thermosynechococcus elongatus BP-1. Comparison with the trimer structure gave detailed insights into monomerization-induced changes in both the central trimerization domain and the peripheral regions of the complex. Monomerization-induced loss of red chlorophylls is assigned to a cluster of chlorophylls adjacent to PsaX. Based on our findings, we propose a role of PsaX in the stabilization of red chlorophylls and that lipids of the surrounding membrane present a major source of thermal energy for uphill excitation energy transfer from red chlorophylls to P700.


Assuntos
Proteínas de Bactérias/ultraestrutura , Clorofila/química , Microscopia Crioeletrônica , Complexo de Proteína do Fotossistema I/ultraestrutura , Proteínas de Bactérias/metabolismo , Clorofila/metabolismo , Cristalografia por Raios X , Modelos Moleculares , Complexo de Proteína do Fotossistema I/metabolismo , Conformação Proteica , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Espectrofotometria Ultravioleta , Thermosynechococcus/metabolismo , Thermosynechococcus/ultraestrutura
3.
Int J Phytoremediation ; 21(8): 821-830, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-30784295

RESUMO

The current research was carried out to estimate the potential of water hyacinth (WH) for removal of nine heavy metals (HMs) from three irrigation canals in Nile Delta. Sampling was achieved in monospecific and homogeneous WH stands at three irrigation canals in the study area, and WH biomass was sampled at monthly intervals from April 2014 to November 2014 using five randomly distributed quadrats (each 0.5 × 0.5 m) at each canal. All HM concentrations were significantly higher in the roots compared with the other WH organs. The WH was recognized by a bioaccumulation factor >1.0 for all HMs. The WH was recognized by translocation factor <1.0 for all HMs (except Pb). In many cases, the concentrations of the HMs in the different organs of WH were correlated with the same HMs in the water. Such correlations indicate that WH reflects the cumulative influences of environmental pollution from the water, and thereby suggesting its potential use in the bio-monitoring of most examined HMs. In conclusion, WH is a promising macrophyte for remediation of irrigation canals polluted with Cd, Co, Cr, Cu, Fe, Mn, Ni, Pb, and Zn.


Assuntos
Eichhornia , Metais Pesados/análise , Poluentes Químicos da Água/análise , Biodegradação Ambiental , Egito , Monitoramento Ambiental
4.
Plant Physiol ; 176(2): 1433-1451, 2018 02.
Artigo em Inglês | MEDLINE | ID: mdl-29187568

RESUMO

The monomeric photosystem I-light-harvesting antenna complex I (PSI-LHCI) supercomplex from the extremophilic red alga Cyanidioschyzon merolae represents an intermediate evolutionary link between the cyanobacterial PSI reaction center and its green algal/higher plant counterpart. We show that the C. merolae PSI-LHCI supercomplex is characterized by robustness in various extreme conditions. By a combination of biochemical, spectroscopic, mass spectrometry, and electron microscopy/single particle analyses, we dissected three molecular mechanisms underlying the inherent robustness of the C. merolae PSI-LHCI supercomplex: (1) the accumulation of photoprotective zeaxanthin in the LHCI antenna and the PSI reaction center; (2) structural remodeling of the LHCI antenna and adjustment of the effective absorption cross section; and (3) dynamic readjustment of the stoichiometry of the two PSI-LHCI isomers and changes in the oligomeric state of the PSI-LHCI supercomplex, accompanied by dissociation of the PsaK core subunit. We show that the largest low light-treated C. merolae PSI-LHCI supercomplex can bind up to eight Lhcr antenna subunits, which are organized as two rows on the PsaF/PsaJ side of the core complex. Under our experimental conditions, we found no evidence of functional coupling of the phycobilisomes with the PSI-LHCI supercomplex purified from various light conditions, suggesting that the putative association of this antenna with the PSI supercomplex is absent or may be lost during the purification procedure.


Assuntos
Complexos de Proteínas Captadores de Luz/química , Complexos de Proteínas Captadores de Luz/metabolismo , Complexo de Proteína do Fotossistema I/química , Complexo de Proteína do Fotossistema I/metabolismo , Rodófitas/fisiologia , Adaptação Biológica , Clorofila/metabolismo , Dicroísmo Circular , Cianobactérias/química , Cianobactérias/fisiologia , Evolução Molecular , Concentração de Íons de Hidrogênio , Luz , Rodófitas/química , Espectrometria de Fluorescência , Temperatura , Zeaxantinas/metabolismo
5.
Artigo em Inglês | MEDLINE | ID: mdl-28213141

RESUMO

The performance of solar energy conversion into alternative energy sources in artificial systems highly depends on the thermostability of photosystem I (PSI) complexes Terasaki et al. (2007), Iwuchukwu et al. (2010), Kothe et al. (2013) . To assess the thermostability of PSI complexes from the thermophilic cyanobacterium Thermosynechococcus elongatus heating induced perturbations on the level of secondary structure of the proteins were studied. Changes were monitored by Fourier transform infrared (FT-IR) spectra in the mid-IR region upon slow heating (1°C per minute) of samples in D2O phosphate buffer (pD 7.4) from 20°C to 100°C. These spectra showed distinct changes in the Amide I region of PSI complexes as a function of the rising temperature. Absorbance at the Amide I maximum of PSI monomers (centered around 1653cm-1), gradually dropped in two temperature intervals, i.e. 60-75 and 80-90°C. In contrast, absorbance at the Amide I maximum of PSI trimers (around 1656cm-1) dropped only in one temperature interval 80-95°C. The thermal profile of the spectral shift of α-helices bands in the region 1656-1642cm-1 confirms the same two temperature intervals for PSI monomers and only one interval for trimers. Apparently, the observed absorbance changes at the Amide I maximum during heating of PSI monomers and trimers are caused by deformation and unfolding of α-helices. The absence of absorbance changes in the interval of 20-65°C in PSI trimers is probably caused by a greater stability of protein secondary structure as compared to that in monomers. Upon heating above 80°C a large part of α-helices both in trimers and monomers converts to unordered and aggregated structures. Spectral changes of PSI trimers and monomers heated up to 100°C are irreversible due to protein denaturation and non-specific aggregation of complexes leading to new absorption bands at 1618-1620cm-1. We propose that monomers shield the denaturation sensitive sides at the monomer/monomer interface within a trimer, making the oligomeric structure more stable against thermal stress.


Assuntos
Cianobactérias/metabolismo , Complexo de Proteína do Fotossistema I/química , Multimerização Proteica , Temperatura , Amidas/química , Desnaturação Proteica , Estabilidade Proteica , Espectroscopia de Infravermelho com Transformada de Fourier
6.
Phys Chem Chem Phys ; 16(24): 11936-41, 2014 Jun 28.
Artigo em Inglês | MEDLINE | ID: mdl-24647437

RESUMO

The improvement of Z-scheme inspired biophotovoltaics is achieved by fine tuning the properties of redox hydrogels applied as immobilization and electron conducting matrices for the photosystem-protein complexes. The formal potentials of the redox hydrogels are adjusted to the respective redox sites in the photosystems for optimized electron transfer without substantial voltage loss. The anode is based on photosystem 2 (PS2) integrated in a phenothiazine modified redox hydrogel with a formal potential of -1 mV vs. SHE, which is 59 mV more positive than the QB acceptor site in PS2. The cathode is based on photosystem 1 (PS1) contacted via an Os-complex based redox hydrogel with a formal potential of 395 mV vs. SHE, i.e. 28 mV more negative than the primary P700 electron acceptor of PS1. The potential difference between the two redox hydrogels is 396 mV. An open circuit voltage (VOC) of 372.5 ± 2.1 mV could be achieved for the biophotovoltaic cell. The maximum power output is 1.91 ± 0.56 µW cm(-2) and the conversion efficiency (η) is 4.5 × 10(-5), representing a 125-fold improvement in comparison to the previously proposed device exploiting the photosynthetic Z-scheme for electrical energy production.


Assuntos
Fontes de Energia Elétrica , Hidrogéis/química , Luz , Oxirredução , Fotossíntese
7.
Biochemistry ; 49(23): 4740-51, 2010 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-20359245

RESUMO

Until now, the functional and structural characterization of monomeric photosystem 1 (PS1) complexes from Thermosynechococcus elongatus has been hampered by the lack of a fully intact PS1 preparation; for this reason, the three-dimensional crystal structure at 2.5 A resolution was determined with the trimeric PS1 complex [Jordan, P., et al. (2001) Nature 411 (6840), 909-917]. Here we show the possibility of isolating from this cyanobacterium the intact monomeric PS1 complex which preserves all subunits and the photochemical activity of the isolated trimeric complex. Moreover, the equilibrium between these complexes in the thylakoid membrane can be shifted by a high-salt treatment in favor of monomeric PS1 which can be quantitatively extracted below the phase transition temperature. Both monomers and trimers exhibit identical posttranslational modifications of their subunits and the same reaction centers but differ in the long-wavelength antenna chlorophylls. Their chlorophyll/P700 ratio (108 for the monomer and 112 for the trimer) is slightly higher than in the crystal structure, confirming mild preparation conditions. Interaction of antenna chlorophylls of the monomers within the trimer leads to a larger amount of long-wavelength chlorophylls, resulting in a higher photochemical activity of the trimers under red or far-red illumination. The dynamic equilibrium between monomers and trimers in the thylakoid membrane may indicate a transient monomer population in the course of biogenesis and could also be the basis for short-term adaptation of the cell to changing environmental conditions.


Assuntos
Cianobactérias/química , Cianobactérias/fisiologia , Complexo de Proteína do Fotossistema I/química , Complexo de Proteína do Fotossistema I/fisiologia , Cristalização , Subunidades Proteicas/genética , Subunidades Proteicas/fisiologia , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Relação Estrutura-Atividade , Tilacoides/química , Tilacoides/fisiologia
8.
Biochim Biophys Acta ; 1767(6): 732-41, 2007 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-17321489

RESUMO

Core antenna and reaction centre of photosystem I (PS I) complexes from the cyanobacteria Arthrospira platensis and Thermosynechococcus elongatus have been characterized by steady-state polarized absorption spectroscopy, including linear dichroism (LD) and circular dichroism (CD). CD spectra and the second derivatives of measured 77 K CD spectra reveal the spectral components found in the polarized absorption spectra indicating the excitonic origin of the spectral forms of chlorophyll in the PS I complexes. The CD bands at 669-670(+), 673(+), 680(-), 683-685(-), 696-697(-), and 711(-) nm are a common feature of used PSI complexes. The 77 K CD spectra of the trimeric PS I complexes exhibit also low amplitude components around 736 nm for A. platensis and 720 nm for T. elongatus attributed to red-most chlorophylls. The LD measurements indicate that the transition dipole moments of the red-most states are oriented parallel to the membrane plane. The formation of P700(+)A(1)(-) or (3)P700 was monitored by time-resolved difference absorbance and LD spectroscopy to elucidate the spectral properties of the PS I reaction centre. The difference spectra give strong evidence for the delocalization of the excited singlet states in the reaction centre. Therefore, P700 cannot be considered as a dimer but should be regarded as a multimer of the six nearly equally coupled reaction centre chlorophylls in accordance with structure-based calculations. On the basis of the results presented in this work and earlier work in the literature it is concluded that the triplet state is localized most likely on P(A), whereas the cation is localized most likely on P(B).


Assuntos
Cianobactérias/metabolismo , Complexo de Proteína do Fotossistema I/metabolismo , Análise Espectral/métodos , Absorção , Clorofila/metabolismo , Dicroísmo Circular
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