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Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774, Moreno, C., Costa C., Moura I., Legall J., Liu M. Y., Payne W. J., Van Dijk C., and Moura J. J. , Eur J Biochem, Feb 15, Volume 212, Number 1, p.79-86, (1993) AbstractWebsite

The electron-transfer kinetics between three different mediators and the hexahemic enzyme nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774) were investigated by cyclic voltammetry and by chronoamperometry. The mediators, methyl viologen, Desulfovibrio vulgaris (Hildenborough) cytochrome c3 and D. desulfuricans (ATCC 27774) cytochrome c3 differ in structure, redox potential and charge. The reduced form of each mediator exchanged electrons with nitrite reductase. Second-order rate constants, k, were calculated on the basis of the theory for a simple catalytic mechanism and the results, obtained by cyclic voltammetry, were compared with those obtained by chronoamperometry. Values for k are in the range 10(6)-10(8) M-1 s-1 and increase in the direction D. desulfuricans cytochrome c3-->D. vulgaris cytochrome c3-->methyl viologen. An explanation is advanced on the basis of electrostatic interactions and relative orientation between the partners involved. Chronoamperometry (computer controlled) offers advantages over cyclic voltammetry in the determination of homogeneous rate constants (faster, more accurate and better reproducibility). Direct, unmediated electrochemical responses of the hexaheme nitrite reductase were also reported.

Redox properties of Desulfovibrio gigas [Fe3S4] and [Fe4S4] ferredoxins and heterometal cubane-type clusters formed within the [Fe3S4] core. Square wave voltammetric studies, Moreno, C., Macedo A. L., Moura I., Legall J., and Moura J. J. , J Inorg Biochem, Feb 15, Volume 53, Number 3, p.219-34, (1994) AbstractWebsite

The same polypeptide chain (58 amino acids, 6 cysteines) is used to build up two ferredoxins in Desulfovibrio gigas a sulfate reducing organism. Ferredoxin II (FdII) contains a single [Fe3S4] core and ferredoxin I (FdI) mainly a [Fe4S4] core. The [Fe3S4] core can readily be interconverted into a [Fe4S4] complex (J.J.G. Moura, I. Moura, T.A. Kent, J.D. Lipscomb, B.H. Huynh, J. LeGall, A.V. Xavier, and E. Munck, J. Biol. Chem. 257, 6259 (1982)). This interconversion process suggested that the [Fe3S4] core could be used as a synthetic precursor for the formation of heterometal clusters. Co, Zn, Cd, and Ni derivatives were produced (I. Moura, J.J.G. Moura, E. Munck, V. Papaephthymiou, and J. LeGall, J. Am. Chem. Soc. 108, 349 (1986), K. Sureurs, E. Munck, I. Moura, J.J.G. Moura, and J. LeGall, J. Am. Chem. Soc. 109, 3805 (1986), and A.L. Macedo, I. Moura, J.J.G. Moura, K. Surerus, and E. Munck, unpublished results). The redox properties of a series of heterometal clusters (MFe3S4] are assessed using direct electrochemistry (square wave voltammetry--SWV) promoted by Mg(II) at a glassy carbon electrode (derivatives: Cd (-495 mV), Fe (-420 mV), Ni (-360 mV), and Co (-245 mV) vs normal hydrogen electrode (NHE)). In parallel, the electrochemical behavior (cyclic voltammetry--CV, differential pulse voltammetry--DPV and SWV) of FdI and FdII were investigated as well as the cluster interconversion process. In addition to the +1/0 (3Fe cluster) and +2/+1 (4Fe cluster) redox transitions, a very negative redox step, at -690 mV, was detected for the 3Fe core, reminiscent of a postulated further 2e- reduction step, as proposed for D. africanus ferredoxin III by F.A. Armstrong, S.J. George, R. Cammack, E.C. Hatchikian, and A.J. Thomson, Biochem. J. 264, 265 (1989). The electrochemical redox potential values are compared with those determined by independent methods (namely by electron paramagnetic resonance (EPR) and visible spectroscopy).

Effects of molybdate and tungstate on expression levels and biochemical characteristics of formate dehydrogenases produced by Desulfovibrio alaskensis NCIMB 13491, Mota, C. S., Valette O., Gonzalez P. J., Brondino C. D., Moura J. J., Moura I., Dolla A., and Rivas M. G. , J Bacteriol, Jun, Volume 193, Number 12, p.2917-23, (2011) AbstractWebsite

Formate dehydrogenases (FDHs) are enzymes that catalyze the formate oxidation to carbon dioxide and that contain either Mo or W in a mononuclear form in the active site. In the present work, the influence of Mo and W salts on the production of FDH by Desulfovibrio alaskensis NCIMB 13491 was studied. Two different FDHs, one containing W (W-FDH) and a second incorporating either Mo or W (Mo/W-FDH), were purified. Both enzymes were isolated from cells grown in a medium supplemented with 1 muM molybdate, whereas only the W-FDH was purified from cells cultured in medium supplemented with 10 muM tungstate. We demonstrated that the genes encoding the Mo/W-FDH are strongly downregulated by W and slightly upregulated by Mo. Metal effects on the expression level of the genes encoding the W-FDH were less significant. Furthermore, the expression levels of the genes encoding proteins involved in molybdate and tungstate transport are downregulated under the experimental conditions evaluated in this work. The molecular and biochemical properties of these enzymes and the selective incorporation of either Mo or W are discussed.

The mechanism of formate oxidation by metal-dependent formate dehydrogenases, Mota, C. S., Rivas M. G., Brondino C. D., Moura I., Moura J. J., Gonzalez P. J., and Cerqueira N. M. , J Biol Inorg Chem, Dec, Volume 16, Number 8, p.1255-68, (2011) AbstractWebsite

Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C-H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results.

The Role Of Nickel And Iron Sulfur Centers In The Bioproduction Of Hydrogen, Moura, J. J. G., Teixeira M., and Moura I. , Pure and Applied Chemistry, May, Volume 61, Number 5, p.915-921, (1989) AbstractWebsite
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Isolation of P590 from Methanosarcina barkeri: evidence for the presence of sulfite reductase activity, Moura, J. J., Moura I., Santos H., Xavier A. V., Scandellari M., and Legall J. , Biochem Biophys Res Commun, Oct 15, Volume 108, Number 3, p.1002-9, (1982) AbstractWebsite
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Enzymatic activity mastered by altering metal coordination spheres, Moura, I., Pauleta S. R., and Moura J. J. , J Biol Inorg Chem, Nov, Volume 13, Number 8, p.1185-95, (2008) AbstractWebsite

Metalloenzymes control enzymatic activity by changing the characteristics of the metal centers where catalysis takes place. The conversion between inactive and active states can be tuned by altering the coordination number of the metal site, and in some cases by an associated conformational change. These processes will be illustrated using heme proteins (cytochrome c nitrite reductase, cytochrome c peroxidase and cytochrome cd1 nitrite reductase), non-heme proteins (superoxide reductase and [NiFe]-hydrogenase), and copper proteins (nitrite and nitrous oxide reductases) as examples. These examples catalyze electron transfer reactions that include atom transfer, abstraction and insertion.

Isolation and characterization of desulforedoxin, a new type of non-heme iron protein from Desulfovibrio gigas, Moura, I., Bruschi M., Legall J., Moura J. J., and Xavier A. V. , Biochem Biophys Res Commun, Apr 25, Volume 75, Number 4, p.1037-44, (1977) AbstractWebsite
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Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin, Moura, I., Teixeira M., Legall J., and Moura J. J. , J Inorg Biochem, Nov, Volume 44, Number 2, p.127-39, (1991) AbstractWebsite

The single iron site of rubredoxin was replaced by nickel and cobalt. The near-infrared/visible/UV spectra of these metal derivatives show ligand-field transitions and charge-transfer bands which closely resemble those of simple tetrathiolate complexes, indicating a tetrahedral arrangement of the sulfur cysteinyl ligands around the metal core. The 1H NMR spectra of the nickel and cobalt derivatives reveal extremely low-field contact shifted resonances of one proton intensity assigned to beta-CH2 and alpha-CH cysteinyl protons. Other well resolved resonances shifted out of the main protein spectral envelope are also observed and probably arise from contact plus pseudocontact shift mechanisms. Rubredoxins from different sulfate reducers were metal substituted and assignments of aliphatic protons are tentatively proposed, taking advantage of the amino acid sequence homologies. The present data is promising in terms of structural analysis of the coordination sphere of the metal core. It was also shown that replacement of the iron atom of desulforedoxin, a close analogue of rubredoxin, by cobalt and nickel was possible.

NMR studies of a dihaem cytochrome from Pseudomonas perfectomarinus (ATCC 14405), Moura, I., Liu M. C., Legall J., Peck, H. D. Jr., Payne W. J., Xavier A. V., and Moura J. J. , Eur J Biochem, Jun 1, Volume 141, Number 2, p.297-303, (1984) AbstractWebsite

Pseudomonas perfectomarinus (ATCC 14405) dihaem cytochrome c552 was studied by 300-MHz proton magnetic resonance. Some of the haem resonances were assigned in the fully reduced and fully oxidized states. No evidence was found for methionine haem axial coordination. The oxidation-reduction equilibrium was studied in detail. Due to the large difference in mid-point redox potential between the two haems (+174 mV, for haem II and -180 mV for haem I) an intermediate oxidation state could be obtained containing reduced haem I and oxidized haem II. In this way the total paramagnetic shift at different oxidation levels could be decomposed in the intrinsic and extrinsic contributions. It was found that the two haems interact. The rate of electron exchange is slow on the NMR time scale. The redox equilibria are discussed for four possible redox species in solution.

A molybdenum-containing (2Fe, 2S) protein from desulphovibrio gigas, a sulphate reducer, Moura, J. J. G., Xavier A. V., Bruschi M., Legall J., and Cabral J. M. P. , Journal of the Less Common Metals, Volume 54, Number 2, p.555-562, (1977) AbstractWebsite
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A bird’s-eye view of denitrification in relation to the nitrogen cycle, Moura, I., Maia L. B., Pauleta S. R., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., Cambridge, p.1-10, (2017) n_cycle-rsc_book-denitrification-chap_1.pdf
Nuclear-magnetic-resonance studies of Desulfuromonas acetoxidans cytochrome c551.5 (c7), Moura, José J. G., Moore Geoffrey R., Williams Robert J. P., Probst Irmelin, Legall Jean, and Xavier António V. , European Journal of Biochemistry, Volume 144, Number 3, p.433-440, (1984) AbstractWebsite

1H nuclear magnetic resonance (NMR) spectroscopy has been used to examine cytochrome c551.5 (c7) from the sulfur reducer, Desulfuromonas acetoxidans. This protein contains three hemes. Two stable oxidation states (the fully oxidized and the fully reduced) as well as intermediate oxidation states were studied. The axial ligands of the iron were found to be neutral histidines. The redox properties of cytochrome c7 were examined and good quantitative agreement found between the NMR results and previously reported redox potential measurements. The properties of cytochrome c7 are discussed together with those of the homologous tetraheme cytochromes c3 isolate from sulfate-reducing bacteria.

Structural control of the redox potentials and of the physiological activity by oligomerization of ferredoxin, Moura, J. J., Xavier A. V., Hatchikian E. C., and Legall J. , FEBS Lett, May 1, Volume 89, Number 1, p.177-9, (1978) AbstractWebsite
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Evidence for the formation of a cobalt-iron-sulfur (CoFe3S4) cluster in Desulfovibrio gigas ferredoxin II, Moura, Isabel, Moura Jose J. G., Munck Eckard, Papaefthymiou Vasilios, and Legall Jean , Journal of the American Chemical Society, 1986/01/01, Volume 108, Number 2, p.349-351, (1986) AbstractWebsite
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Nitrate and nitrite utilization in sulfate-reducing bacteria, Moura, I., Bursakov S., Costa C., and Moura J. J. , Anaerobe, Oct, Volume 3, Number 5, p.279-90, (1997) AbstractWebsite
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Mossbauer And Electron-Paramagnetic-Res Studies Of Desulforedoxin From Desulfovibrio-Gigas, Moura, I., Huynh B. H., Hausinger R. P., Legall J., Xavier A. V., and Munck E. , Journal of Biological Chemistry, 1980, Volume 255, Number 6, p.2493-2498, (1980) AbstractWebsite
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[20] Low-spin sulfite reductases, Moura, Isabel, and Lino Ana Rosa , Methods in Enzymology, Volume Volume 243, p.296-303, (1994) Abstract
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Spectroscopic characterization of a high-potential monohaem cytochrome from Wolinella succinogenes, a nitrate-respiring organism. Redox and spin equilibria studies, Moura, I., Liu M. Y., Costa C., Liu M. C., Pai G., Xavier A. V., Legall J., Payne W. J., and Moura J. J. , Eur J Biochem, Nov 15, Volume 177, Number 3, p.673-82, (1988) AbstractWebsite

When purified, a high-potential c-type monohaem cytochrome from the nitrate-respiring organism, Wollinella succinogenes (VPI 10659), displayed a minimum molecular mass of 8.2 kDa and 0.9 mol iron and 0.95 mol haem groups/mol protein. Visible light spectroscopy suggested the presence of an equilibrium between two ligand arrangements around the haem, i.e. an absorption band at 695 nm characteristic of haem-methionine coordination (low-spin form) coexisting with a high-spin form revealed by a band at 619 nm and a shoulder at 498 nm. The mid-point redox potential measured by visible redox titration of the low-spin form was approximately +100 mV. Binding cyanide (Ka = 5 x 10(5) M-1) resulted in the displacement of the methionyl axial residue, and full conversion to a low-spin, cyanide-bound form. Structural features were studied by 300-MHz 1H-NMR spectroscopy. In the oxidized state, the pH dependence of the haem methyl resonances (pH range 5-10) and the magnetic susceptibility measurements (using an NMR method) were consistent with the visible light spectroscopic data for the presence of a high-spin/low-spin equilibrium with a transition pKa of 7.3. The spin equilibrium was fast on the NMR time scale. The haem methyl resonances presented large downfield chemical shifts. An unusually broad methyl resonance at around 35 ppm (pH = 7.5, 25 degrees C) was extremely temperature-dependent [delta(323 K) - delta(273 K) = 7.2 ppm] and was assigned to the S-CH3 group of the axial methionine. In the ferrous state only a low-spin form is present. The haem meso protons, the methyl group and the methylene protons from the axial methionine were identified in the reduced form. The resonances from the aromatic residues (three tyrosines and one phenylalanine) were also assigned. Detailed monitoring of the NMR-redox pattern of the monohaem cytochrome from the fully reduced up to the fully oxidized state revealed that the rate of the intermolecular electronic exchange process was approximately 6 x 10(6) M-1 s-1 at 303 K and pH = 6.31. A dihaem cytochrome also present in the crude cell extract and purified to a homogeneous state, exhibited a molecular mass of 11 kDa and contained 2.43 mol iron and 1.89 mol haem c moieties/mol cytochrome. The absorption spectrum in the visible region exhibited no band at 695 nm, suggesting that methione is not a ligand for either of the two haems. Recovery of only small amounts of this protein prevented more detailed structural analyzes.

Influence of storage solution on enamel demineralization submitted to pH cycling, Moura, J. S., Rodrigues L. K., Del Bel Cury A. A., Lima E. M., and Garcia R. M. , J Appl Oral Sci, Sep, Volume 12, Number 3, p.205-8, (2004) AbstractWebsite

Extracted human teeth are frequently used for research or educational purposes. Therefore, it is necessary to store them in disinfectant solutions that do not alter dental structures. Thus, this study evaluated the influence of storage solution on enamel demineralization. For that purpose, sixty samples were divided into the following groups: enamel stored in formaldehyde (F1), stored in thymol (T1), stored in formaldehyde and submitted to pH cycling (F2), stored in thymol and submitted to pH cycling (T2). All samples were evaluated by cross-sectional microhardness analysis and had their percentage of mineral volume versus micrometer (integrated area) determined. Differences between groups were found up to 30-microm depth from the enamel surface (p < 0.05), where samples from group T2 were more demineralized. It was concluded that the storage solution influenced the reaction of a dental substrate to a cariogenic challenge, suggesting that formaldehyde may increase enamel resistance to demineralization, when compared to demineralization occurring in enamel stored in thymol solution.

A molybdenum-containing iron-sulphur protein from Desulphovibrio gigas, Moura, J. J., Xavier A. V., Bruschi M., Legall J., Hall D. O., and Cammack R. , Biochem Biophys Res Commun, Oct 4, Volume 72, Number 3, p.782-9, (1976) AbstractWebsite
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Ferredoxins, Moura, J. J., Macedo A. L., and Palma P. N. , Methods Enzymol, Volume 243, p.165-88, (1994) AbstractWebsite
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Chromosome aberrations in cattle raised on bracken fern pasture, Moura, J. W., Stocco dos Santos R. C., Dagli M. L., D'Angelino J. L., Birgel E. H., and Becak W. , Experientia, Sep 15, Volume 44, Number 9, p.785-8, (1988) AbstractWebsite

Thirteen cows maintained on natural bracken fern (Pteridium aquilinum) were analyzed cytogenetically. The frequency of structural chromosome aberrations detected in peripheral blood cells was significantly higher when compared to that detected in animals raised on pasture containing no bracken fern. We discuss the clastogenic action of fern and its synergistic action with infection by type 2 and 4 papilloma virus in the same animals.

Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mossbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II, Moura, J. J., Moura I., Kent T. A., Lipscomb J. D., Huynh B. H., Legall J., Xavier A. V., and Munck E. , J Biol Chem, Jun 10, Volume 257, Number 11, p.6259-67, (1982) AbstractWebsite
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Proteins containing the factor F430 from methanosarcina barkeri and methanobacterium thermoautotrophicum: Isolation and properties, Moura, Isabel, Moura José J. G., Santos Helena, Xavier Antonio V., Burch Gary, Peck Jr Harry D., and Legall Jean , Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Volume 742, Number 1, p.84-90, (1983) AbstractWebsite
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