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Observation of ligand-based redox chemistry at the active site of a molybdenum enzyme, George, G. N., Costa C., Moura J. J. G., and Moura I. , Journal of the American Chemical Society, Mar 24, Volume 121, Number 11, p.2625-2626, (1999) AbstractWebsite
On the active sites of the [NiFe] hydrogenase from Desulfovibrio gigas. Mossbauer and redox-titration studies, Huynh, B. H., Patil D. S., Moura I., Teixeira M., Moura J. J., Dervartanian D. V., Czechowski M. H., Prickril B. C., Peck, H. D. Jr., and Legall J. , J Biol Chem, Jan 15, Volume 262, Number 2, p.795-800, (1987) AbstractWebsite

The [NiFe] hydrogenase isolated from Desulfovibrio gigas was poised at different redox potentials and studied by Mossbauer spectroscopy. The data firmly establish that this hydrogenase contains four prosthetic groups: one nickel center, one [3Fe-xS], and two [4Fe-4S] clusters. In the native enzyme, both the nickel and the [3Fe-xS] cluster are EPR-active. At low temperature (4.2 K), the [3Fe-xS] cluster exhibits a paramagnetic Mossbauer spectrum typical for oxidized [3Fe-xS] clusters. At higher temperatures (greater than 20 K), the paramagnetic spectrum collapses into a quadrupole doublet with parameters magnitude of delta EQ magnitude of = 0.7 +/- 0.06 mm/s and delta = 0.36 +/- 0.06 mm/s, typical of high-spin Fe(III). The observed isomer shift is slightly larger than those observed for the three-iron clusters in D. gigas ferredoxin II (Huynh, B. H., Moura, J. J. G., Moura, I., Kent, T. A., LeGall, J., Xavier, A. V., and Munck, E. (1980) J. Biol. Chem. 255, 3242-3244) and in Azotobacter vinelandii ferredoxin I (Emptage, M. H., Kent, T. A., Huynh, B. H., Rawlings, J., Orme-Johnson, W. H., and Munck, E. (1980) J. Biol. Chem. 255, 1793-1796) and may indicate a different iron coordination environment. When D. gigas hydrogenase is poised at potentials lower than -80 mV (versus normal hydrogen electrode), the [3Fe-xS] cluster is reduced and becomes EPR-silent. The Mossbauer data indicate that the reduced [3Fe-xS] cluster remains intact, i.e. it does not interconvert into a [4Fe-4S] cluster. Also, the electronic properties of the reduced [3Fe-xS] cluster suggest that it is magnetically isolated from the other paramagnetic centers.

One Electron Reduced Square Planar Bis(benzene-1,2-dithiolato) Copper Dianionic Complex and Redox Switch by O2/HO-, Maiti, B. K., Maia L. B., Pal K., Pakira B., Aviles T., Moura I., Pauleta S. R., Nuñez J. L., Rizzi A. C., Brondino C. D., Sarkar S., and Moura J. J. G. , Inorg Chem, Volume 53, p.12799-12808, (2014)
Orange protein from Desulfovibrio alaskensis G20: insights into the Mo-Cu cluster protein-assisted synthesis, Carepo, M. S., Carreira C., Grazina R., Zakrzewska M. E., Dolla A., Aubert C., Pauleta S. R., Moura J. J. G., and Moura I. , J Biol Inorg Chem, Volume 21, p.53-62, (2016)
Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxin, Auchere, F., Sikkink R., Cordas C., Raleiras P., Tavares P., Moura I., and Moura J. J. , J Biol Inorg Chem, Oct, Volume 9, Number 7, p.839-49, (2004) AbstractWebsite

Superoxide reductases are a class of non-haem iron enzymes which catalyse the monovalent reduction of the superoxide anion O2- into hydrogen peroxide and water. Treponema pallidum (Tp), the syphilis spirochete, expresses the gene for a superoxide reductase called neelaredoxin, having the iron protein rubredoxin as the putative electron donor necessary to complete the catalytic cycle. In this work, we present the first cloning, overexpression in Escherichia coli and purification of the Tp rubredoxin. Spectroscopic characterization of this 6 kDa protein allowed us to calculate the molar absorption coefficient of the 490 nm feature of ferric iron, epsilon=6.9+/-0.4 mM(-1) cm(-1). Moreover, the midpoint potential of Tp rubredoxin, determined using a glassy carbon electrode, was -76+/-5 mV. Reduced rubredoxin can be efficiently reoxidized upon addition of Na(2)IrCl(6)-oxidized neelaredoxin, in agreement with a direct electron transfer between the two proteins, with a stoichiometry of the electron transfer reaction of one molecule of oxidized rubredoxin per one molecule of neelaredoxin. In addition, in presence of a steady-state concentration of superoxide anion, the physiological substrate of neelaredoxin, reoxidation of rubredoxin was also observed in presence of catalytic amounts of superoxide reductase, and the rate of rubredoxin reoxidation was shown to be proportional to the concentration of neelaredoxin, in agreement with a bimolecular reaction, with a calculated k(app)=180 min(-1). Interestingly, similar experiments performed with a rubredoxin from the sulfate-reducing bacteria Desulfovibrio vulgaris resulted in a much lower value of k(app)=4.5 min(-1). Altogether, these results demonstrated the existence for a superoxide-mediated electron transfer between rubredoxin and neelaredoxin and confirmed the physiological character of this electron transfer reaction.

Oxidation-reduction potentials of the hemes in cytochrome C3 from Desulfovibrio gigas in the presence and absence of ferredoxin by EPR spectroscopy, Xavier, A. V., Moura J. J., Legall J., and Dervartanian D. V. , Biochimie, Volume 61, Number 5-6, p.689-95, (1979) AbstractWebsite

1. Ferricytochrome c3 from D. gigas exhibits two low-spin ferric heme EPR resonances with gz-values at 2.959 and 2.853. Ferrocytochrome c3 is diamagnetic based on the absence of any EPR signals. 2. EPR potentiometric titrations result in the resolution of the two low-spin ferric heme resonances into two additional heme components representing in total the four hemes of the cytochrome, with EM values of -235 mV and -315 mV at heme resonance I and EM values of -235 mV and -306 mV at heme resonance II. 3. EPR spectroscopy has detected a significant diminution of intensity (approx. 60 p. 100) in the gx amplitude of ferricytochrome c3 in the presence of D. gigas ferredoxin II. The presence of ferredoxin II also causes a more negative shift in the EM of the second components of the signals at heme resonances I and II of cytochrome C3. Both observations suggest that an interaction has occurred between cytochrome C3 and ferredoxin II. 4. The results presented suggest that the heme ligand environment of ferricytochrome c3 from D. gigas is less perturbed and/or less asymmetric than environment for ferricytochrome c3 from D. vulgaris whose EPR behavior indicates the non-equivalence of all four hemes.

Oxidation-reduction studies of the Mo-(2Fe-2S) protein from Desulfovibrio gigas, Moura, J. J., Xavier A. V., Cammack R., Hall D. O., Bruschi M., and Legall J. , Biochem J, Aug 1, Volume 173, Number 2, p.419-25, (1978) AbstractWebsite

Potentiometric titration followed by e.p.r. measurements were used to determine the midpoint reduction potentials of the redox centres of a molybdenum-containing iron-sulphur protein previously isolated from Desulfovibrio gigas, a sulphate-reducing bacterium (Moura, Xavier, Bruschi, Le Gall, Hall & Cammack (1976) Biochem. Biophys. Res. Commun. 728 782-789; Moura, Xavier, Bruschi, Le Gall & Cabral (1977) J. Less Common Metals 54, 555-562). The iron-sulphur centres could readily be distinguished into three types by means of g values, temperature effect, oxidation-reduction potential values and reduction rates. The type-I Fe-S centres are observed at 77 K. They show mid-point potential values of -260mV (Fe-S type IA) and -440 mV (Fe-S type IB). Centres of types IA and IB appear to have similar spectra at 77 K and 24 K. The Fe-S type-II centres are only observed below 65 K and have a midpoint potential of -28mV. Long equilibration times (30 min) with dye mediators under reducing conditions were necessary to observe the very slow equilibrating molybdenum signals. The potential values associated with this signal were estimated to be approx. -415 mV for Mo(VI)/Mo(V) and-530mV for Mo(V)/Mo(IV).

Oxovanadium(IV) and amino acids—VI. The systems glycylglycine and glycylglycylglycine + VO2+; a potentiometric and spectroscopic study, Pessoa, Costa J., Luz S. M., Duarte R., Moura J. J. G., and Gillard R. D. , Polyhedron, Volume 12, Number 23, p.2857-2867, (1993) AbstractWebsite
Oxovanadium(IV) complexes of the dipeptides glycyl-L-aspartic acid, L-aspartylglycine and related ligands; a spectroscopic and potentiometric study, Pessoa, J. C., Gajda T., Gillard R. D., Kiss T., Luz S. M., Moura J. J. G., Tomaz I., Telo J. P., and Torok I. , Journal of the Chemical Society-Dalton Transactions, Nov 7, Number 21, p.3587-3600, (1998) AbstractWebsite

The equilibria in the systems VO2+ + L (L = Gly-L-Asp, L-Asp-Gly, N-acetyl-L-aspartic acid or succinic acid) have been studied at 25 degrees C and 0.2 mol dm(3) K(CI) medium by a combination of potentiometric and spectroscopic methods (ESR, circular dichroism and visible absorption). Formation constants were calculated from pH-metric data with total oxovanadium(Iv) concentrations of(0.6-4) x 10(-3) mol dm(-3) and ligand-to-metal (L:M) ratios of 2-8 (AspGly) or 4-15: 1 (other systems). The position of the Asp residue in the peptide chain affects the co-ordination mode of the ligands: while in the GlyAsp system bis complexes start to form at pH less than 2, for AspGly only 1 : 1 complexes form, with relatively high CD signal. The co-ordination behaviour of N-acetyl-L-aspartic and succinic acids is similar. The results of potentiometric and spectroscopic methods are self consistent. Isomeric structures are discussed for each stoichiometry proposed and the results compared with those for L-aspartic acid and dipeptides with non-coordinating side chains.