Rosa, AM, Lobo AM, Branco PS, Prabhakar S, SadaCosta M.
1997.
New syntheses of the Amaryllidacaea alkaloids vasconine, assoanine, oxoassoanine, pratosine and ismine by radical cyclisation, JAN 6. TETRAHEDRON. 53:299-306., Number 1
Abstractn/a
Duarte, RO, Reis AR, Girio F, Moura I, Moura JJ, Collaco TA.
1997.
The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum-containing protein, Jan 3. Biochem Biophys Res Commun. 230:30-4., Number 1
AbstractThe formate dehydrogenase (FDH) isolated from cells of Methylobacterium sp. RXM grown on molybdenum-containing mineral medium using methanol as carbon source, was partially purified (at least 90% pure as revealed by SDS-PAGE). The enzyme is unstable under oxygen and all the purification steps were conducted under strict anaerobic conditions. The molecular mass is 75 kDa (gel exclusion 300 kDa). The enzyme was characterized in terms of the kinetic parameters towards different substrates and electron acceptors, pH and temperature dependence and the effect of a wide range of compounds in the enzymatic activity. The EPR spectra of the dithionite reduced sample show, at low temperature (below 20 K), two rhombic EPR signals due to two distinct [Fe-S] centres (centre I at g-values 2.023, 1.951 and 1.933, and centre II at g-values 2.054 and 1.913). At high temperature (around 100 K) another rhombic EPR signal is optimally observed at g-values 2.002, 1.987 and 1.959 and attributed to the molybdenum site. The EPR signals assigned to the iron-sulfur centres show a strong analogy with the aldehyde oxido-reductase from Desulfovibrio gigas known to contain a Mo-pterin and two [2Fe-2S] centres and whose crystallographic structure was recently resolved.
Yu, L, Kennedy M, Czaja C, Tavares P, Moura JJ, Moura I, Rusnak F.
1997.
Conversion of desulforedoxin into a rubredoxin center, Feb 24. Biochem Biophys Res Commun. 231:679-82., Number 3
AbstractRubredoxin and desulforedoxin both contain an Fe(S-Cys)4 center. However, the spectroscopic properties of the center in desulforedoxin differ from rubredoxin. These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated highspin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin.
Franco, R, Calvete JJ, Thole HH, Raida M, Moura I, Moura JJG.
1997.
The primary structure of the beta subunit of Desulfovibrio desulfuricans (ATCC 27774) NiFe hydrogenase, Apr. Protein and Peptide Letters. 4:131-138., Number 2
AbstractThe periplasmic [NiFe] hydrogenase isolated from Desulfovibrio (D.) desulfuricans (ATCC 27774) is a heterodimer of a 28 kDa (beta) and a 60 kDa (alpha) subunit. Here we report the complete amino acid sequence of the small (beta) polypeptide chain determined by Edman degradation of proteolytic fragments. Electrospray-ionization mass spectrometry of the native protein confirmed the sequencing results. The sequence is compared with that of D. gigas [NiFe] hydrogenase whose three-dimensional structure has been recently published.
Yu, L, Kennedy M, Czaja C, Tavares P, Moura JJG, Moura I, Rusnak F.
1997.
Conversion of desulforedoxin into a rubredoxin center. Biochemical And Biophysical Research Communications. {231}:{679-682}., Number {3}
AbstractRubredoxin and desulforedoxin both contain an Fe(S-Cys)(4) center, However the spectroscopic properties of the center in desulforedoxin differ from rubredoxin, These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated high-spin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin. (C) 1997 Academic Press.
Romao, MJ, Kolln I, Dias JM, Carvalho AL, Romero A, Varela PF, Sanz L, Topfer-Petersen E, Calvete JJ.
1997.
Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 angstrom resolution: a bovine polypeptide of the spermadhesin family. Journal of Molecular Biology. 274:650-660., Number 4
Abstractn/a