Photosynthetic proteins for technological applications

Giardi, Maria Teresa; Pace, Emanuela

doi:10.1016/j.tibtech.2005.03.003

Cited by 90 publications

(75 citation statements)

References 35 publications

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“…Recently, chlorophyll fluorescence is used as one of the sensitive parameters for biosensors using thylakoid membranes or algal cells as the transducers Dobrikova et al 2009;Giardi & Pace, 2005;Koblizek et al, 1998;Misra et al, , 2006Misra et al, , 2011Raskov et al, 2011;Vladkova et al, 2009Vladkova et al, , 2011. Besides this fast Chl fluorescence can be used as a sensitive device for detection of ion/ salt sensitivity and other environmental stress factors (Misra et al, 2001a(Misra et al, ,b, 2007.…”

Section: Applications Of Chlorophyll Fluorescence Measurements In Plamentioning

confidence: 99%

Chlorophyll Fluorescence in Plant Biology

Misra¹,

Misra²,

Singh³

2012

Biophysics

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Section: Applications Of Chlorophyll Fluorescence Measurements In Plamentioning

confidence: 99%

Chlorophyll Fluorescence in Plant Biology

Misra¹,

Misra²,

Singh³

2012

Biophysics

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“…[2][3][4][5][6] Utilizing a unique cysteine (Cys) mutation at the end of PS I, we demonstrate a four-step chemical procedure based on carbodiimide chemistry for covalent binding of PS I proteins to carbon nanotubes (CNTs). [7] The method allows studying hybrid nanosystems for the construction of optoelectronic devices based on PSI-CNTs heterostructures.…”

mentioning

confidence: 99%

A Photosynthetic Reaction Center Covalently Bound to Carbon Nanotubes

Carmeli¹,

Mangold²,

Frolov³

et al. 2007

Advanced Materials

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The photosystem I (PS I) reaction center is a chlorophyll protein complex located in thylakoid membranes of chloroplasts and cyanobacteria. PS I mediates a light-induced electron transfer through a serial of redox reactions.[1] It is intriguing to incorporate the PS I into optoelectronic circuits, since the PS I exhibits outstanding optoelectronic properties found only in the photosynthetic systems. The quantum yield for absorbing a photon within the whole complex is determined to be close to 100 %, while the energy yield for the process is approximately 58 %.[1] The nanoscale dimension and the generation of 1 V photovoltage further makes the PS I reaction center a promising unit for applications in molecular optoelectronics. [2][3][4][5][6] Utilizing a unique cysteine (Cys) mutation at the end of PS I, we demonstrate a four-step chemical procedure based on carbodiimide chemistry for covalent binding of PS I proteins to carbon nanotubes (CNTs). [7] The method allows studying hybrid nanosystems for the construction of optoelectronic devices based on PSI-CNTs heterostructures. Three variations in the design of PSI-CNT hybrid structures are presented which allow exploiting the potential of PS I as an integrated part of CNT nanodevice for optoelectronic applications. Recently, we have demonstrated the possibility to covalently bind PS I directly to gold surfaces [5] and indirectly via a small linker molecule to GaAs surfaces. [6] To this end, amino acids in the extra membrane loops of the PS I facing the cytoplasmic side of the bacterial membrane (oxidizing side) were mutated to cysteines (Cys) enabling the formation of covalent bonds with a metal surface or a chemically functionalized GaAs surface. The Cys located at extra membranal loops of the protein do not have steric hindrance, when placed on a solid surface e.g. of a gold electrode or CNTs as shown here.The mutations D235C/Y634C were selected near the special chlorophyll pair P700 to allow close proximity between the reaction center and the CNTs. [5] As depicted by white arrows in Figure 1, here we utilize a PS I with two mutants on the oxidizing side of the PS I. This single sided mutant ensures a high outcome of our chemical self-assembly procedure. For a variation of our chemical scheme we also use bipolar (BM) mutants, where the mutations are located at both the oxidizing (white arrows) and the reducing side of the PS I (gray arrow). Our self-assembly approach facilitates efficient electronic junctions and avoids disturbance in the function of the reaction center. The covalent attachment of the PS I through the Cys further ensures the structural stability of the self-assembled, oriented PS I. As demonstrated recently, [5,6] a dry oriented monolayer of PS I assembled on gold electrodes and GaAs surfaces exhibits charge transfer between PS I and the solid state surface. In this work, we extend the above chemical scheme in order to covalently attach PS I proteins to CNTs. The hybrid systems are characterized by atomic force microscopy and COMMUNICATION

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“…Properly assembled biosensors can satisfy these requirements, also providing reliability and flexibility of the assays (Giardi & Pace, 2005). A major difficulty in estimating environmental quality related to herbicides contamination is due to seasonal change of field application and the extremely low levels of the maximum admissible concentrations set by the EC.…”

Section: Description Of Analytical Methods and Biosensors For Herbicimentioning

confidence: 99%