Fortunato, E., Nuno Correia, Pedro Barquinha, Claudia Costa, Luis Pereira, Goncalo Goncalves, and Rodrigo Martins. "
Paper Field Effect Transistor."
Zinc Oxide Materials and Devices Iv. Eds. F. H. Teherani, C. W. Litton, and D. J. Rogers. Vol. 7217. Proceedings of SPIE, 7217. 2009.
Abstractn/a
Martins, R., L. Pereira, P. Barquinha, I. Ferreira, R. Prabakaran, G. GONCALVES, A. Goncalves, and E. Fortunato. "
Zinc oxide and related compounds: order within the disorder."
Zinc Oxide Materials and Devices Iv. Eds. F. H. Teherani, C. W. Litton, and D. J. Rogers. Vol. 7217. Proceedings of SPIE, 7217. 2009.
Abstractn/a
Conrath, Katja, Alice S. Pereira, Carlos E. Martins, Cristina G. Timoteo, Pedro Tavares, Silvia Spinelli, Joerg Kinne, Christophe Flaudrops, Christian Cambillau, Serge Muyldermans, Isabel Moura, Jose J. G. Moura, Mariella Tegoni, and Aline Desmyter. "
{Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase}."
Protein science : a publication of the Protein Society. 18 (2009): 619-628.
AbstractNitric Oxide Reductase (NOR) is an integral membrane protein performing the reduction of NO to N2O. NOR is composed of two subunits: the large one (NorB) is a bundle of 12 transmembrane helices (TMH). It contains a b type heme and a binuclear iron site, which is believed to be the catalytic site, comprising a heme b and a non-hemic iron. The small subunit (NorC) harbors a cytochrome c and is attached to the membrane through a unique TMH. With the aim to perform structural and functional studies of NOR, we have immunized dromedaries with NOR and produced several antibody fragments of the heavy chain (VHHs, also known as nanobodies (TM)). These fragments have been used to develop a faster NOR purification procedure, to proceed to crystallization assays and to analyze the electron transfer of electron donors. BIAcore experiments have revealed that up to three VHHs can bind concomitantly to NOR with affinities in the nanomolar range. This is the first example of the use of VHHs with an integral membrane protein. Our results indicate that VHHs are able to recognize with high affinity distinct epitopes on this class of proteins, and can be used as versatile and valuable tool for purification, functional study and crystallization of integral membrane proteins.
Rivas, Maria G., Cristiano S. Mota, Sofia R. Pauleta, Marta S. P. Carepo, Filipe Folgosa, Susana L. A. Andrade, Guy Fauque, Alice S. Pereira, Pedro Tavares, Juan J. Calvete, Isabel Moura, and Jose J. G. Moura. "
{Isolation and characterization of a new Cu-Fe protein from Desulfovibrio aminophilus DSM12254.}."
Journal Of Inorganic Biochemistry. 103 (2009): 1314-1322.
AbstractThe isolation and characterization of a new metalloprotein containing Cu and Fe atoms is reported. The as-isolated Cu-Fe protein shows an UV-visible spectrum with absorption bands at 320 nm, 409 nm and 615 nm. Molecular mass of the native protein along with denaturating electrophoresis and mass spectrometry data show that this protein is a multimer consisting of 14+/-1 subunits of 15254.3+/-7.6 Da. Mössbauer spectroscopy data of the as-isolated Cu-Fe protein is consistent with the presence of [2Fe-2S](2+) centers. Data interpretation of the dithionite reduced protein suggest that the metallic cluster could be constituted by two ferromagnetically coupled [2Fe-2S](+) spin delocalized pairs. The biochemical properties of the Cu-Fe protein are similar to the recently reported molybdenum resistance associated protein from Desulfovibrio, D. alaskensis. Furthermore, a BLAST search from the DNA deduced amino acid sequence shows that the Cu-Fe protein has homology with proteins annotated as zinc resistance associated proteins from Desulfovibrio, D. alaskensis, D. vulgaris Hildenborough, D. piger ATCC 29098. These facts suggest a possible role of the Cu-Fe protein in metal tolerance.