Thoenes, U, Flores OL, Neves A, Devreese B, Van Beeumen JJ, Huber R, Romao MJ, Legall J, Moura JJ, Rodrigues-Pousada C.
1994.
Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase, Mar 15. Eur J Biochem. 220:901-10., Number 3
AbstractIn 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 almost identical to a calculated codon usage of the Desulfovibrio bacteria.
Ferreira, GC, Franco R, Lloyd SG, Pereira AS, Moura I, Moura JJ, Huynh BH.
1994.
Mammalian ferrochelatase, a new addition to the metalloenzyme family, Mar 11. J Biol Chem. 269:7062-5., Number 10
AbstractA [2Fe-2S] cluster has been detected in mammalian ferrochelatase, the terminal enzyme of the heme biosynthetic pathway. Natural ferrochelatase, purified from mouse livers, and recombinant ferrochelatase, purified from an overproducing strain of Escherichia coli, were investigated by electron paramagnetic resonance (EPR) and Mossbauer spectroscopy. In their reduced forms, both the natural and recombinant ferrochelatases exhibited an identical EPR signal with g values (g = 2.00, 1.93, and 1.90) and relaxation properties typical of [2Fe-2S]+ cluster. Mossbauer spectra of the recombinant ferrochelatase, purified from a strain of E. coli cells transformed with a plasmid encoding murine liver ferrochelatase and grown in 57Fe-enriched medium, demonstrated unambiguously that the cluster is a [2Fe-2S] cluster. No change in the cluster oxidation state was observed during catalysis. The putative protein binding site for the Fe-S cluster in mammalian ferrochelatases is absent from the sequences of the bacterial and yeast enzymes, suggesting a possible role of the [2Fe-2S] center in regulation of mammalian ferrochelatases.
Ferreira, GC, Franco R, Lloyd SG, Pereira AS, Moura I, Moura JJG, Huynh BH.
1994.
MAMMALIAN FERROCHELATASE, A NEW ADDITION TO THE METALLOENZYME FAMILY. Journal Of Biological Chemistry. {269}:{7062-7065}., Number {10}, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
AbstractA [2Fe-2S] cluster has been detected in mammalian ferrochelatase, the terminal enzyme of the heme biosynthetic pathway. Natural ferrochelatase, purified from mouse livers, and recombinant ferrochelatase, purified from an overproducing strain of Escherichia coli, were investigated by electron paramagnetic resonance (EPR) and Mossbauer spectroscopy. In their reduced forms, both the natural and recombinant ferrochelatases exhibited an identical EPR signal with g values (g = 2.00, 1.93, and 1.90) and relaxation properties typical of [2Fe-2S](+) cluster. Mossbauer spectra of the recombinant ferrochelatase, purified from a strain of E. coli cells transformed with a plasmid encoding murine liver ferrochelatase and grown in Fe-57-enriched medium, demonstrated unambiguously that the cluster is a [2Fe-2S] cluster. No change in the cluster oxidation state was observed during catalysis, The putative protein binding site for the Fe-S cluster in mammalian ferrochelatases is absent from the sequences of the bacterial and yeast enzymes, suggesting a possible role of the [2Fe-2S] center in regulation of mammalian ferrochelatases.
Thoenes, U, Flores OL, Neves A, Devreese B, Van Beeumen JJ, Huber R, Romao MJ, Legall J, Moura JJG, Rodriguespousada C.
1994.
MOLECULAR-CLONING AND SEQUENCE-ANALYSIS OF THE GENE OF THE MOLYBDENUM-CONTAINING ALDEHYDE OXIDOREDUCTASE OF DESULFOVIBRIO-GIGAS - THE DEDUCED AMINO-ACID-SEQUENCE SHOWS SIMILARITY TO XANTHINE DEHYDROGENASE. European Journal of Biochemistry. 220:901-910., Number 3
Abstractn/a
Saraiva, LM, Fauque G, Besson S, Moura I.
1994.
Physico-chemical and Spectroscopic Properties of the Monohemic Cytochrome C552 from Pseudomonas nautica 617. European Journal of Biochemistry. 224:1011-1017., Number 3: Blackwell Science Ltd
AbstractA c-type monohemic ferricytochrome c552 (11 kDa) was isolated from the soluble extract of a marine denitrifier, Pseudomonas nautica strain 617, grown under anaerobic conditions with nitrate as final electron acceptor. The NH2-terminal sequence and the amino acid composition of the cytochrome were determined. The heme iron of the cytochrome c552 has histidine-methionine as axial ligands, and a pH-dependent mid-point redox potential, equal to 250 mV at pH 7.6. The presence of methionine was demonstrated by visible, EPR and NMR spectroscopies. The assignment of most of the hemic protons was performed applying two-dimensional NOE spectroscopy (NOESY), and the aromatic region was assigned through two-dimensional correlated spectroscopy (COSY) experiments. The EPR spectrum of the oxidised form of the cytochrome c552 is typical of a low-spin ferric heme.