6 documents found, page 1 of 1
Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The...
Cunha, Carlos A.; Macieira, Sofia; Dias, João M.; Almeida, Gabriela; Gonçalves, Luísa L.; Costa, Cristina; Lampreia, Jorge; Huber, RobertThe gene encoding cytochrome c nitrite reductase (NrfA) from Desulfovibrio desulfuricans ATCC 27774 was sequenced and the crystal structure of the enzyme was determined to 2.3-Å resolution. In comparison with homologous structures, it presents structural differences mainly located at the regions surrounding the putative substrate inlet and product outlet, and includes a well defined second calcium site with oct...
The isolation and characterization of cytochrome c nitrite reductase subunits (...
Almeida, Maria Gabriela; Macieira, Sofia; Gonçalves, Luisa L.; Huber, Robert; Cunha, Carlos A.; Romão, Maria João; Costa, Cristina; Lampreia, JorgeThe cytochrome c nitrite reductase is isolated from the membranes of the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 as a heterooligomeric complex composed by two subunits (61 kDa and 19 kDa) containing c-type hemes, encoded by the genes nrfA and nrfH, respectively. The extracted complex has in average a. 2NrfA:1NrfH composition. The separation of ccNiR subunits from one another is accompl...
Gene sequence and the 1.8 Å crystal structure of the tungsten-containing format...
Raaijmakers, Hans; Macieira, Sofia; Dias, João M.; Teixeira, Susana; Bursakov, Sergey; Huber, Robert; Moura, José J. G.; Moura, Isabel; Romão, Maria J.We thank the EMBL Grenoble Outstation, beamline BM-14, for MAD measurements at the ESRF under the European Union TMR/LSF Program. Hans Bartunik and Gleb Bourenkov are acknowledged for help at the BW6 beamline of the MPG-ASMB in DESY, Hamburg, for collecting the first FDH native data set. The Institute for Genomic Research (TIGR) is kindly acknowledged for making the preliminary sequence data on the Desulfovibri...
A structure-based catalytic mechanism for the xanthine oxidase family of molybd...
Huber, Robert; Hof, Peter; Duarte, Rui O.; Moura, Jose J. G.; Moura, Isabel; Liu, Ming Yih; LeGall, Jean; Hille, Russ; Archer, MargaridaThe crystal structure of the xanthine oxidase-related molybdenum-iron protein aldehyde oxidoreductase from the sulfate reducing anaerobic Gram- negative bacterium Desulfovibrio gigas (Mop) was analyzed in its desulfo-, sulfo-, oxidized, reduced, and alcohol-bound forms at 1.8-Å resolution. In the sulfo-form the molybdenum molybdopterin cytosine dinucleotide cofactor has a dithiolenebound fac-[Mo, =O, =S, ···(OH...
Molecular cloning and sequence analysis of the gene of the molybdenum‐containin...
Thoenes, Ulrich; Flores, Orfeu L.; Neves, Ana; Devreese, Bart; van Beeumen, Jozef J.; Huber, Robert; Romão, Maria J.; LeGall, Jean; Moura, José J.G.In this report, we describe the isolation of a 4020‐bp genomic PstI fragment of Desulfovibrio gigas harboring the aldehyde oxido‐reductase gene. The aldehyde oxido‐reductase gene spans 2718 bp of genomic DNA and codes for a protein with 906 residues. The protein sequence shows an average 52% (± 1.5%) similarity to xanthine dehydrogenase from different organisms. The codon usage of the aldehyde oxidoreductase is...
Subunit composition, crystallization and preliminary crystallographic studies o...
Romão, Maria J.; Barata, Belarmino A. S.; Archer, Margarida; Lobeck, Karin; Moura, Isabel; CARRONDO, Maria A.; LeGall, Jean; Lottspeich, FriedrichThe Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe‐2S] centers. The enzyme was characterized by SDS/PAGE, gel‐filtration and analytical ultracentrifugation experiments. It was crystallized at 4°C, pH 7.2, using isopropanol and MgCl 2 as precipitants. The crystals diffract beyond 0.3‐nm (3.0‐Å) resolution and belong to space group P6 1 22 or its enantiomorph, ...