Resonance Raman spectra of rubredoxin, desulforedoxin, and the synthetic analog Fe(S2-o-xyl)2: conformational effects,
Yachandra, Vittal K., Hare Jeffrey, Moura I., and Spiro Thomas G.
, Journal of the American Chemical Society, 1983/10/01, Volume 105, Number 21, p.6455-6462, (1983)
Abstractn/a
Resonance Raman spectra of rubredoxin: new assignments and vibrational coupling mechanism from iron-54/iron-56 isotope shifts and variable-wavelength excitation,
Czernuszewicz, Roman S., Legall Jean, Moura Isabel, and Spiro Thomas G.
, Inorganic Chemistry, 1986/02/01, Volume 25, Number 5, p.696-700, (1986)
Abstractn/a
Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas,
Johnson, M. K., Hare J. W., Spiro T. G., Moura J. J., Xavier A. V., and Legall J.
, J Biol Chem, Oct 10, Volume 256, Number 19, p.9806-8, (1981)
AbstractThe resonance Raman spectra of ferredoxins (Fd) I and II from Desulfovibrio gigas are reported using 4579 A Ar+ laser excitation. The (3Fe-3S) center in Fd II has a characteristic resonance Raman spectrum, readily distinguishable from those of (2Fe-2S) or (4Fe-4S) clusters. Reduction of Fd II produces a marked alteration in the resonance Raman spectrum. Fd I is shown to contain both (3Fe-3S) and (4Fe-4S) Fd-type clusters. The results illustrate the potential of resonance Raman spectroscopy in Fe-S cluster identification, even in cases where more than one cluster type is present.
Resonance Raman studies of nickel tetrathiolates and nickel-substituted rubredoxins and desulforedoxin,
Huang, Yun Hua, Moura Isabel, Moura Jose J. G., Legall Jean, Park Jae Bum, Adams Michael W. W., and Johnson Michael K.
, Inorganic Chemistry, 1993/02/01, Volume 32, Number 4, p.406-412, (1993)
Abstractn/a
Resonance Raman study on the iron-sulfur centers of Desulfovibrio gigas aldehyde oxidoreductase,
Zhelyaskov, V., Yue K. T., Legall J., Barata B. A., and Moura J. J.
, Biochim Biophys Acta, Oct 25, Volume 1252, Number 2, p.300-4, (1995)
AbstractResonance Raman spectra of the molybdenum containing aldehyde oxidoreductase from Desulfovibrio gigas were recorded at liquid nitrogen temperature with various excitation wavelengths. The spectra indicate that all the iron atoms are organised in [2Fe-2S] type centers consistent with cysteine ligations. No vibrational modes involving molybdenum could be clearly identified. The features between 280 and 420 cm-1 are similar but different from those of typical plant ferredoxin-like [2Fe-2S] cluster. The data are consistent with the presence of a plant ferredoxin-like cluster (center I) and a unique [2Fe-2S] cluster (center II), as suggested by other spectroscopic studies. The Raman features of center II are different from those of other [2Fe-2S] clusters in proteins. In addition, a strong peak at ca. 683 cm-1, which is not present in other [2Fe-2S] clusters in proteins, was observed with purple excitation (406.7-413.1 nm). The peak is assigned to enhanced cysteinyl C-S stretching in center II, suggesting a novel geometry for this center.
Revisiting the catalytic CuZ cluster of nitrous oxide (N2O) reductase. Evidence of a bridging inorganic sulfur,
Brown, K., Djinovic-Carugo K., Haltia T., Cabrito I., Saraste M., Moura J. J., Moura I., Tegoni M., and Cambillau C.
, J Biol Chem, Dec 29, Volume 275, Number 52, p.41133-6, (2000)
AbstractNitrous-oxide reductases (N2OR) catalyze the two-electron reduction of N(2)O to N(2). The crystal structure of N2ORs from Pseudomonas nautica (Pn) and Paracoccus denitrificans (Pd) were solved at resolutions of 2.4 and 1.6 A, respectively. The Pn N2OR structure revealed that the catalytic CuZ center belongs to a new type of metal cluster in which four copper ions are liganded by seven histidine residues. A bridging oxygen moiety and two other hydroxide ligands were proposed to complete the ligation scheme (Brown, K., Tegoni, M., Prudencio, M., Pereira, A. S., Besson, S., Moura, J. J. G., Moura, I., and Cambillau, C. (2000) Nat. Struct. Biol. 7, 191-195). However, in the CuZ cluster, inorganic sulfur chemical determination and the high resolution structure of Pd N2OR identified a bridging inorganic sulfur instead of an oxygen. This result reconciles the novel CuZ cluster with the hitherto puzzling spectroscopic data.
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)
Abstractn/a
Role of vitamin B12 in methyl transfer for methane biosynthesis by Methanosarcina barkeri,
Wood, J. M., Moura I., Moura J. J., Santos M. H., Xavier A. V., Legall J., and Scandellari M.
, Science, Apr 16, Volume 216, Number 4543, p.303-5, (1982)
AbstractWhen Methanosarcina barkeri is grown on methanol as the sole carbon source, a B12-containing protein is synthesized by this organism. This B12 protein contains bound aquocobalamin, and when this cofactor is reduced and methylated with [14C]methyl iodide, the resultant [14C]methyl B12 protein is extremely active in the biosynthesis of 14C-labeled methane. These findings indicate that a B12-dependent system is operative in the biological formation of methane in addition to other systems that are B12-independent.
Rubredoxin as a paramagnetic relaxation-inducing probe,
Almeida, R. M., Pauleta S. R., Moura I., and Moura J. J.
, J Inorg Biochem, Sep, Volume 103, Number 9, p.1245-53, (2009)
AbstractThe paramagnetic effect due to the presence of a metal center with unpaired electrons is no longer considered a hindrance in protein NMR spectroscopy. In the present work, the paramagnetic effect due to the presence of a metal center with unpaired electrons was used to map the interface of an electron transfer complex. Desulfovibrio gigas cytochrome c(3) was chosen as target to study the effect of the paramagnetic probe, Fe-rubredoxin, which produced specific line broadening in the heme IV methyl resonances M2(1) and M18(1). The rubredoxin binding surface in the complex with cytochrome c(3) was identified in a heteronuclear 2D NMR titration. The identified heme methyls on cytochrome c(3) are involved in the binding interface of the complex, a result that is in agreement with the predicted complexes obtained by restrained molecular docking, which shows a cluster of possible solutions near heme IV. The use of a paramagnetic probe in (1)HNMR titration and the mapping of the complex interface, in combination with a molecular simulation algorithm proved to be a valuable strategy to study electron transfer complexes involving non-heme iron proteins and cytochromes.
Rubredoxin mutant A51C unfolding dynamics: A Forster Resonance Energy Transfer study,
Santos, Andrea, Duarte Americo G., Fedorov Alexander, Martinho Jose M. G., and Moura Isabel
, Biophysical Chemistry, May, Volume 148, Number 1-3, p.131-137, (2010)
AbstractThe unfolding dynamics of the rubredoxin mutant A51C (RdA51C) from Desulfovibrio vulgaris (DvRd) was studied on the temperature range from 25 degrees C to 90 degrees C and by incubation at 90 degrees C. By Forster Resonance Energy Transfer (FRET) the donor (D; Trp37) to acceptor (A; 1,5-IAEDANS) distance distribution was probed at several temperatures between 25 degrees C and 90 degrees C, and incubation times at 90 degrees C. From 25 degrees C to 50 degrees C the half-width distributions values (hw) are small and the presence of a discrete D-A distance was considered. At temperatures higher than 60 degrees C broader hw values were observed reflecting the existence of a distance distribution. The protein denaturation was only achieved by heating the solution for 2 h at 90 degrees C, as probed by the increase of the D-A mean distance. From Trp fluorescence it was shown that its vicinity was maintained until similar to 70 degrees C, being the protein hydrodynamic radius invariant until 50 degrees C. However, at similar to 70 degrees C a change in the partial unfolding kinetics indicates the disruption of specific H-bonds occurring in the hydrophobic core. The red shift of 13 nm, observed on the Trp37 emission, confirms the exposition of Trp to solvent after protein incubation at 90 degrees C for 2.5 h. (C) 2010 Elsevier B.V. All rights reserved.
Sample treatment for protein identification by mass spectrometry-based techniques,
Lopez-Ferrer, D., Canas B., Vazquez J., Lodeiro C., Rial-Otero R., Moura I., and Capelo J. L.
, Trac-Trends in Analytical Chemistry, Nov, Volume 25, Number 10, p.996-1005, (2006)
AbstractRapid identification of proteins is of primary importance for the analytical community. Protein-biomarker discovery for medical diagnostics or pharmacological purposes is becoming one of the hottest research topics. Moreover, rapid identification of proteins can help unambiguous bacterial and virus detection. In addition, the fast identification of bacteria can be used to beat bioterrorism. As a consequence, new analytical methodologies have emerged recently with the aim of making protein analysis as fast and as confident as possible. In this article, we critically review the new trends in sample treatment for protein identification and comment on the prospects for the future in this promising analytical area. (c) 2006 Elsevier Ltd. All rights reserved.
Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly,
Carvalho, R., Almeida R., Moura J. J. G., Lourenço N., Fonseca L., and Cordas C. M.
, Chemistry Select, Volume 1, p.6546–6552, (2016)
Sarcoplasmic reticulum calcium ATPase is inhibited by organic vanadium coordination compounds: pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an amavadine analogue,
Aureliano, M., Henao F., Tiago T., Duarte R. O., Moura J. J., Baruah B., and Crans D. C.
, Inorg Chem, Jul 7, Volume 47, Number 13, p.5677-84, (2008)
AbstractThe general affinity of the sarcoplasmic reticulum (SR) Ca (2+)-ATPase was examined for three different classes of vanadium coordination complexes including a vanadium(V) compound, pyridine-2,6-dicarboxylatodioxovanadium(V) (PDC-V(V)), and two vanadium(IV) compounds, bis(maltolato)oxovanadium(IV) (BMOV), and an analogue of amavadine, bis( N-hydroxylamidoiminodiacetato)vanadium(IV) (HAIDA-V(IV)). The ability of vanadate to act either as a phosphate analogue or as a transition-state analogue with enzymes' catalysis phosphoryl group transfer suggests that vanadium coordination compounds may reveal mechanistic preferences in these classes of enzymes. Two of these compounds investigated, PDC-V(V) and BMOV, were hydrolytically and oxidatively reactive at neutral pH, and one, HAIDA-V(IV), does not hydrolyze, oxidize, or otherwise decompose to a measurable extent during the enzyme assay. The SR Ca (2+)-ATPase was inhibited by all three of these complexes. The relative order of inhibition was PDC-V(V) > BMOV > vanadate > HAIDA-V(IV), and the IC 50 values were 25, 40, 80, and 325 microM, respectively. Because the observed inhibition is more potent for PDC-V(V) and BMOV than that of oxovanadates, the inhibition cannot be explained by oxovanadate formation during enzyme assays. Furthermore, the hydrolytically and redox stable amavadine analogue HAIDA-V(IV) inhibited the Ca (2+)-ATPase less than oxovanadates. To gauge the importance of the lipid environment, studies of oxidized BMOV in microemulsions were performed and showed that this system remained in the aqueous pool even though PDC-V(V) is able to penetrate lipid interfaces. These findings suggest that the hydrolytic properties of these complexes may be important in the inhibition of the calcium pump. Our results show that two simple coordination complexes with known insulin enhancing effects can invoke a response in calcium homeostasis and the regulation of muscle contraction through the SR Ca (2+)-ATPase.
Screening of Potential Stress Biomarkers in Sweat Associated with Sports Training,
Nunes, M. J., Cordas C. M., Moura J. J. G., Noronha J. P., and Branco L. C.
, Sports Medicine - Open, Volume 7, p.8, (2021)
Screen‐Printed Electrodes Testing for Detection of Potential Stress Biomarkers in Sweat,
M.J., Nunes, G.N. Valério, A. Samhan‐Arias, J.J.G. Moura, C. Rouco, Sousa J. P., and C.M. Cordas
, Electrocatalysis, Volume 13, p.299–305, (2022)
SERR spectroelectrochemical study of cytochrome cd1 nitrite reductase co-immobilized with physiological redox partner cytochrome c552 on biocompatible metal electrodes,
Silveira, C. M., Quintas P. O., Moura I., Moura J. J. G., Hildebrandt P., Almeida M. G., and Todorovic S.
, Plos One, Volume 10, p.e0129940, (2015)
Simplifying sample handling for protein identification by peptide mass fingerprint using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry,
Cordeiro, Francisco M., Carreira Ricardo J., Rial-Otero Raquel, Rivas Gabriela M., Moura Isabel, and Capelo Jose-Luis
, Rapid Communications in Mass Spectrometry, 2007, Volume 21, Number 20, p.3269-3278, (2007)
AbstractAn ultrasonic bath, an ultrasonic probe and a sonoreactor were used to speed up the kinetics of the reactions involved in each step of the sample handling for in-gel protein identification by peptide mass fingerprint, PMF, using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The following steps were successfully accelerated using ultrasonic energy: gel washing, protein reduction, and protein alkylation. As a result, a reduction comprising 80% to 90% of the total time involved in the classic approach was achieved. In addition the sample handling was also drastically simplified. The number of peptides identified and the protein sequence coverage obtained for the new procedure were comparable to those obtained with the traditional sample treatment for the following protein standards: glycogen phosphorylase b, BSA, ovalbumin, carbonic anhydrase, trypsin inhibitor and alpha-lactalbumin. Finally, as a proof of the procedure, specific proteins were identified from complex protein mixtures obtained from three different sulphate- reducing bacteria: Desulfovibrio, desulfuricans G20, Desulfuvibrio gigas NCIB 9332, and Desulfuvibrio desulfuricans ATCC 27774. Copyright (c) 2007 John Wiley & Sons, Ltd.
Simulation of the electrochemical behavior of multi-redox systems. Current potential studies on multiheme cytochromes,
Moreno, C., Campos A., Teixeira M., Legall J., Montenegro M. I., Moura I., Van Dijk C., and Moura J. G.
, Eur J Biochem, Dec 5, Volume 202, Number 2, p.385-93, (1991)
AbstractThe direct unmediated electrochemical response of the tetrahemic cytochrome c3 isolated from sulfate reducers Desulfovibrio baculatus (DSM 1743) and D. vulgaris (strain Hildenborough), was evaluated using different electrode systems [graphite (edge cut), gold, semiconductor (InO2) and mercury)] and different electrochemical methods (cyclic voltammetry and differential pulse voltammetry). A computer program was developed for the theoretical simulation of a complete cyclic voltammetry curve, based on the method proposed by Nicholson and Shain [Nicholson, R.S. & Shain, I. (1964) Anal. Chem. 36, 706-723], using the Gauss-Legendre method for calculation of the integral equations. The experimental data obtained for this multi-redox center protein was deconvoluted in to the four redox components using theoretically generated cyclic voltammetry curves and the four mid-point reduction potentials determined. The pH dependence of the four reduction potentials was evaluated using the deconvolution method described.
A single histidine is required for activity of cytochrome c peroxidase from Paracoccus denitrificans,
McGinnity, D. F., Devreese B., Prazeres S., Van Beeumen J., Moura I., Moura J. J., and Pettigrew G. W.
, J Biol Chem, May 10, Volume 271, Number 19, p.11126-33, (1996)
AbstractThe diheme cytochrome c peroxidase from Paracoccus denitrificans was modified with the histidine-specific reagent diethyl pyrocarbonate. At low excess of reagent, 1 mol of histidine was modified in the oxidized enzyme, and modification was associated with loss of the ability to form the active state. With time, the modification reversed, and the ability to form the active state was recovered. The agreement between the spectrophotometric measurement of histidine modification and radioactive incorporation using a radiolabeled reagent indicated little modification of other amino acids. However, the reversal of histidine modification observed spectrophotometrically was not matched by loss of radioactivity, and we propose a slow transfer of the ethoxyformyl group to an unidentified amino acid. The presence of CN- bound to the active peroxidatic site of the enzyme led to complete protection of the essential histidine from modification. Limited subtilisin treatment of the native enzyme followed by tryptic digest of the C-terminal fragment (residues 251-338) showed that radioactivity was located in a peptide containing a single histidine at position 275. We propose that this conserved residue, in a highly conserved region, is central to the function of the active mixed-valence state.
SiW11Fe@MIL-101(Cr) composite: A novel and versatile electrocatalyst,
Fernandes, D. M., Granadeiro C. M., de M. Paes Sousa. P., Grazina R., Moura J. J. G., Silva P., Almeida Paz F. A., Cunha-Silva L., Balula S. S., and Freire C.
, ChemElectroChem, Volume 1, p.1293-1300, (2014)
Small phospho-donors phosphorylate MorR without inducing protein conformational changes,
Castro, N. S. S., Laia C. A. T., Maiti B. K., Cerqueira N., Moura I., and Carepo M. S. P.
, Biophys Chem, Volume 240, p.25-33, (2018)
The solution structure of a [3Fe-4S] ferredoxin: oxidised ferredoxin II from Desulfovibrio gigas,
Goodfellow, B. J., Macedo A. L., Rodrigues P., Moura I., Wray V., and Moura J. J.
, J Biol Inorg Chem, Aug, Volume 4, Number 4, p.421-30, (1999)
AbstractThe use of standard 2D NMR experiments in combination with 1D NOE experiments allowed the assignment of 51 of the 58 spin systems of oxidised [3Fe4S] ferredoxin isolated from Desulfovibrio gigas. The NMR solution structure was determined using data from 1D NOE and 2D NOESY spectra, as distance constraints, and information from the X-ray structure for the spin systems not detected by NMR in torsion angle dynamics calculations to produce a family of 15 low target function structures. The quality of the NMR family, as judged by the backbone r.m.s.d. values, was good (0.80 A), with the majority of phi/psi angles falling within the allowed region of the Ramachandran plot. A comparison with the X-ray structure indicated that the overall global fold is very similar in solution and in the solid state. The determination of the solution structure of ferredoxin II (FdII) in the oxidised state (FdIIox) opens the way for the determination of the solution structure of the redox intermediate state of FdII (FdII(int)), for which no X-ray structure is available.