Ferreira, I., Aguas Mendes Fernandes Fortunato Martins H. L. F. "
Performances of nano/amorphous silicon films produced by hot wire plasma assisted technique."
Materials Research Society Symposium - Proceedings. Vol. 507. 1999. 607-612.
AbstractThis work reports on the performances of undoped and n doped amorphous/nano-crystalline silicon films grown by hot wire plasma assisted technique. The film's structure (including the presence of several nanoparticles with sizes ranging from 5 nm to 50 nm), the composition (oxygen and hydrogen content) and the transport properties are highly dependent on the filament temperature and on the hydrogen dilution. The undoped films grown under low r.f. power (≈4 mWcm-2) and with filament temperatures around 1850 °K have dark conductivities below 10-10 Scm-1, optical gaps of about 1.5 eV and photo-sensitivities above 105, (under AM1.5), with almost no traces of oxygen content. N-doped silicon films were also fabricated under the same conditions which attained conductivities of about 10-2 Scm-1.
Almendra, MJ, CD Brondino, O. Gavel, AS Pereira, P. Tavares, S. Bursakov, R. Duarte, J. CALDEIRA, JJG Moura, and I. Moura. "
Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
Biochemistry. 38 (1999): 16366-16372.
AbstractAn air-stable formate dehydrogenase (FDH), an enzyme that catalyzes the oxidation of formate to carbon dioxide, was purified from the sulfate reducing organism Desulfovibrio gigas (D. gigas) NCIB 9332. D. gigas FDH is a heterodimeric protein [alpha (92 kDa) and beta (29 kDa) subunits] and contains 7 +/- 1 Fe/protein and 0.9 +/- 0.1 W/protein, Selenium was not detected. The UV/visible absorption spectrum of D, gigas FDH is typical of an iron-sulfur protein. Analysis of pterin nucleotides yielded a content of 1.3 +/- 0.1 guanine monophosphate/mol of enzyme, which suggests a tungsten coordination with two molybdopterin guanine dinucleotide cofactors. Both Mossbauer spectroscopy performed on D. gigas FDH grown in a medium enriched with Fe-57 and EPR studies performed in the native and fully reduced state of the protein confirmed the presence of two [4Fe-4S] clusters. Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d(1) configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.