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.
Schienstock, Gerd, Gotard Bechmann, Joerg Flecker, Ursula Huws, Geert Van Hootegem, Maria Luisa Mirabile, António Moniz, and Sean Ò Siochru Technical Systems, Organisation Forms and Social Implications: Statistical Analysis of the Firm Survey (Second Interim Report). University Library of Munich, Germany, 1999.
AbstractThis is the second interim report of the research project "Information Society, Work and the Generation of New Forms of Social Exclusion" (SOWING). It is based on a firm survey conducted in the eight regions participating in the research project — Flanders (Belgium), Lazio (Italy), Niederösterreich (Austria), Portugal, the Republic of Ireland, the Stuttgart area (Germany), the Tampere region (Finland) and the West London area (U.K.). The aim of this report is to present a broad overview of the collected data. In general, only simple statistical methods have been applied. The report focuses on a regional comparison; however, the data have also been analysed by firm size, measured by quantity of staff, and industrial sector. It should be seen as a first step in the data analysis; it may also give some hints for a more strategic analysis of the survey data.
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.