Bactéria redutoras de sulfato / Bactérias desnitrificantes / metaloproteínas / espectroscopia (RPE, RMN, MB) / sequenciação de proteínas / centros ferro-enxofre / hemos / redutase do nitrito / redutase do nitrato /reductase do óxido nitroso/reductase do óxido nítico/ redutase do formato / novos centros contendo ferro / propriedades redox.
O campo principal de investigação tem sido a aplicação de diferentes técnicas espectroscópicas (UV/visível, RMN, RPE e Mössbauer) ao estudo de metaloproteínas envolvidas em processos metabólicos vários (redução de sulfato, formação de metano e desnitrificação). A compreensão dos percursos metabólicos nestes grupos bacterianos é de grande importância do ponto de vista ecológico e energético.
Nestes últimos anos foi dada uma relevância principal aos processos que conduzem à redução de nitrato devido à sua importâcia, nomeadamente na utilização de compostos contendo azoto pela agricultura e sua degradação nos solos. Os estudos foram dirigidos no sentido de se estabelecerem relações estrutura-função, sendo comparadas diferentes proteínas isoladas de várias estirpes bacterianas.
Os centros activos estudados incluem hemos, centros ferro enxofre (tipo rubredoxina, [2Fe-2S], [3Fe-4S], [4Fe-4S], molibdénio, cobre, cobalto, zinco bem como associações entre centros de ferro enxofre com molibdénio, níquel, sirohemos e flavinas).
Foram sintetizadas a partir do centro de [3Fe-4S] novos agregados do tipo [M, 3Fe-4S] em que M=Co, Ni, Zn, Cd. Proteínas com novos tipos de associações de centros foram também isoladas: rubredoxina e centro do tipo hemeritrina [rubreritina] e centro do tipo desulforedoxina e ferro octaédrico [desulfoferrodoxina].
Uma proteína com um novo tipo de centro ferro enxofre contendo 4Fe e um estado de spin S=9/2 com múltiplas transições redox constituiu uma das descobertas mais recentes e possivelmente com implicações importantes no domínio dos centros de ferro enxofre.
As técnicas espectroscópicas principalmente usadas são RMN, RPE e Mössbauer.
A espectroscopia de RMN tem sido aplicada a proteínas de pequena massa molecular tais como citocromos, rubredoxinas e ferredoxinas. Titulações redox seguidas por RMN no citocromo c3 levaram à conclusão de que alguns hemos estão em interacção. A RMN foi também usada para seguir a interconversão entre um centro de [3Fe-4S] e um centro de [4Fe-4S].
O uso simultâneo de RPE e espectroscopia de Mössbauer tem sido um dos principais objectivos. Uma vez que existe uma forte correlação entre estas duas espectroscopias devido à interação hiperfina electrão-núcleo, um centro activo RPE pode ser inequivocamente identificado e atribuido a uma determinada componente do espectro de Mössbauer. O número de átomos de ferro por centro activo em RPE pode ser determinado correlacionando as intensidades relativas de absorção da componente espectral em Mössbauer, o conteúdo de ferro da amostra e a densidade de spin determinada por RPE.
Este método foi extremamente útil na identificação do centro de 4Fe e levou à descoberta do centro de [3Fe-4S].
Publicações desde 2006
278.BIOCHEMICAL AND SPECTROSCOPIC CHARACTERIZATION OF AN ALDEHYDE
OXIDOREDUCTASE ISOLATED FROM DESULFOVIBRIO aminophilus
A. Thapper, M. G. Rivas, C. D. Brondino, B.Ollivier, G. Fauque, I. Moura and J. J. G. Moura
J.Inorg.Biochem. 100, 44-50 (2006)
279.MOLYBDENUM AND TUNGSTEN ENZYMES:THE XANTHINE OXIDASE FAMILY
C.B.Brondino, M.J.Romão, I.Moura and J.J.G.Moura
Curr. Opinion in Chem. Biology 10, 109-114 (2006)
280. BACTERIAL NITRATE REDUCTASES:MOLECULAR AND BIOLOGICAL ASPECTS OF NITRATE REDUCTION
P.J.González, C.Correia, I.Moura, C.D.Brondino and J.J.G.Moura
J.Inorg.Biochem. 100, 1015-1123 (2006)
281. THE FIRST CRYSTAL STRUCTURE OF CLASS-III SUPEROXIDE REDUCTASE FROM TREPONEMA PALLIDUM
T. Santos-Silva, J. Trincão, A. L. Carvalho, C. Bonifácio, F. Auchère, P. Raleiras, I. Moura, José J.G. Moura and M. J. Romão
J.Biol.Inorg.Chem. 11, 548-558 (2006)
282. KINETIC STUDIES OF THE SUPEROXIDE-MEDIATED ELECTRON TRANSFER REACTIONS BETWEEN RUBREDOXIN-TYPE PROTEINS AND SUPEROXIDE REDUCTASES.
F.Auchère, S. R. Pauleta, P. Tavares, I. Moura and J. J. G. Moura
J.Biol.Inorg.Chem.11, 433-444 (2006)
283. Desulfovibrio gigas FERREDOXIN II: REDOX STRUCTURAL MODULATION OF THE [3Fe-4S] CLUSTER
P.M.Rodrigues, A.L.Macedo, B.J.Goodfellow, I.Moura and J.J.G.Moura
J.Biol.Inorg.Chem. 11, 307-315 (2006)
284. STRUCTURAL AND EPR STUDIES OF MONONUCLEAR MOLYBDENUM ENZYMES FROM SULFATE REDUCING BACTERIA
C.D.Brondino, M.G.Rivas, M. J. Romão, J.J.G.Moura and I. Moura
Accounts of Chemical Research 39,788-96 (2006)
285. EPR AND REDOX PROPERTIES OF PERIPLASMIC NITRATE REDUCTASE FROM
DESULFOVIBRIO DESULFURICANS ATCC 27774
P.J.González, M.G.Rivas, C.Brondino,S.Bursakov, I. Moura, J.J.G.Moura
J.Biol.Inorg.Chem.11, 609-616 (2006)
286. MODELLING THE ELECTRON-TRANSFER COMPLEX BETWEEN ALDEHYDE OXIDOREDUCTASE AND FLAVODOXIN
L.Krippahl, P.N.Palma, I.Moura and J.J.G.Moura
Eur.J.Inorg.Chem. 19, 3835-3840 (2006)
287. NITRIC OXIDE REDUCTASE:DIRECT ELECTROCHEMISTRY AND ELECTROCATALYTIC ACTIVITY
C.Cordas, A.S.Pereira, C.E.Martins, C.G.Timóteo, I.Moura, P.Tavares and J.J.G.Moura
Chem.Biochem. 7, 1878-81 (2006)
288. METALLOENZYMES OF THE DENITRIFICATION PATHWAY
P.Tavares, A.Pereira, J.J.G.Moura and I.Moura
J.of Inorg.Biochem. 100, 2087-2100 (2006)
289. SAMPLE TREATMENT FOR PROTEIN IDENTIFICATION BY MASS
SPECTROMETRY-BASED TECHNIQUES.
D. López-Ferrer, B. Cañas, J. Vázquez, C. Lodeiro, R. Rial-Otero, I. Moura, J. L. Capelo
Trac-Trends in Analytical Chemistry 25, 996-1005 (2006)
290. A NEEDLE IN A HAYSTACK.THE ACTIVE SITE OF THE MEMBRANE-BOUND COMPLEX CYTOCHROME c NITRITE REDUCTASE
M.G.Almeida, C.M.Silveira, B.Guigliarelli, P.Bertrand, J.J.G.Moura, I.Moura and C.Leger
FEBS Lett 581,284-288 (2007)
291. SPECTROSCOPIC, COMPUTATIONAL, AND KINETIC STUDIES OF THE MU(4)-SULFIDE-BRIDGED TETRANUCLEAR CU(Z) CLUSTER IN N(2)O REDUCTASE: PH EFFECT ON THE EDGE LIGAND AND ITS CONTRIBUTION TO REACTIVITY.
Ghosh S, Gorelsky SI, George SD, Chan JM, Cabrito I, Dooley DM,Moura JJ, Moura I, Solomon EI.
J Am Chem Soc.129,3955-3965 (2007 )
292.CHROMATOGRAPHIC-BASED METHODS FOR PESTICIDE DETERMINATION IN HONEY: AN OVERVIEW
R. Rial-Otero, E.M. Gaspar, I. Moura, J.L. Capelo
Talanta 71, 503-514 (2007)
293.SONOREACTOR–BASED TECHNOLOGY FOR FAST HIGH-THROUGHPUT PROTEOLYTIC DIGESTION OF PROTEINS.
R. Rial-Otero, R. J. Carreira, F. M. Cordeiro, A. J. Moro, L. Fernandez, I. Moura, J. L. Capelo.
J Proteome Res. 6, 909-12 (2007)
294.MEDIATED CATALYSIS OF PARACOCCUS PANTOTROPHUS CYTOCHROME C PEROXIDASE BY PARACOCCUS PANTOTROPHUS PSEUDOAZURIN – KINETICS OF INTERMOLECULAR ELECTRON TRANSFER
P. M. Paes de Sousa, S. R. Pauleta, G. W. Pettigrew, I. Moura, J. J. G. Moura, M. M. Correia dos Santos, M. L. Simões Gonçalves
J.Biol.Inorg.Chem 12,691-8 (2007)
295. SUPEROXIDE REDUCTASES
A.S.Pereira, P.Tavares, F.Folgosa, R.M.Almeida, I.Moura and J.J.G.Moura
Eur.J.Inorg.Chem.18, 2569-2581 (2007)
296.DISSIMILATORY NITRATE AND NITRITE AMMONIFICATION BY SULPHATE-REDUCING BACTERIA
José J.G. Moura, Pablo Gonzalez, Isabel Moura and Guy Fauque
in “Sulphate-Reducing Bacteria: Environmental and Engineering Systems”, L.L.Barton and W.A.Hamilton editors, Cambridge University Press (2007)
297.GAS CHROMATOGRAPHY MASS SPECTROMETRY DETERMINATION OF ACARICIDES FROM HONEY AFTER A NEW FAST ULTRASONIC-BASED SOLID PHASE MICRO-EXTRACTION SAMPLE TREATMENT
R. Rial-Otero, E. M. Gaspar, I. Moura, J. L. Capelo.
Talanta 71, 1906-1914 (2007)
298.NEW FINDINGS FOR IN-GEL DIGESTION ACCELERATED BY HIGH INTENSITY FOCUSED ULTRASOUND FOR PROTEIN IDENTIFICATION BY MATRIX ASSISTED LASER DESORPTION IONIZATION TIME-OF-FLIGHT MASS SPECTROMETRY.
R. J. Carreira, F. M. Cordeiro, A. J. Moro, M. G. Rivas, R. Rial-Otero, E. M. Gaspar, I. Moura, J. L. Capelo
J Chromatogr A. 1153(1-2):291-9 (2007) Epub 2006 Oct 10.
299. CRYSTAL STRUCTURE OF THE SIXTEEN HEME CYTOCHROME FROM DESULFOVIBRIO GIGAS: A GLYCOSYLATED PROTEIN IN A SULPHATE REDUCING BACTERIUM
Teresa Santos-Silva, João Miguel Dias, Alain Dolla, Marie-Claire Durand, Luísa L. Gonçalves, Jorge Lampreia, Isabel Moura, Maria João Romão
J.Mol.Biol. 370,659-73 (2007)
300.EPR CHARACTERIZATION OF THE MOLYBDENUM(V) FORMS OF FORMATE DEHYDROGENASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 UPON FORMATE REDUCTION
María G. Rivas, Pablo J. González, Carlos D. Brondino, José J. G. Moura, and Isabel Moura
J.Inorg.Biochem.101, 1617-22 (2007) 2007 May 8; [Epub ahead of print]
301.HETERODIMERIC NITRATE REDUCTASE (NapAB) FROM Cupriavidus necator H16:PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS
C.Coelho, P.J.González, J.Trincão, A.L.Carvalho, S.Najmudin, T.Hetlman, S.Dieckman, J.J.G.Moura, I.Moura and M.J.Romão
Acta Cryst. 63, 516-9 (2007)
302. MODELLING METALLOTHIONEIN INDUCTION IN THE LIVER OF Sparus aurata EXPOSED TO METAL-CONTAMINATED SEDIMENTS
P.M.Costa, T.Repolho, S.Caeiro, M.E.Diniz, I.Moura, M.H.Costa
Ecotoxicol.Environm.Safety (2007), doi:10.1016/j.ecoenv.2007.05.012
303.ULTRASONIC ASSISTED PROTEIN ENZYMATIC DIGESTION FOR FAST PROTEIN IDENTIFICATION BY MATRIX-ASSISTED LASER DESORPTION/IONIZATION TIME-OF-FLIGHT MASS SPECTROMETRY SONOREACTOR VERSUS ULTRASONIC PROBE.
Rial-Otero R, Carreira RJ, Cordeiro FM, Moro AJ, Santos HM, Vale G, Moura I, Capelo JL.
J Chromatogr A. 1166(1-2)101-7 (2007)
304. SIMPLIFYING SAMPLE HANDLING FOR PROTEIN IDENTIFICATION BY PEPTIDE MASS FINGERPRINT USING MATRIX-ASSISTED LASER DESORPTION/IONIZATION TIME-OF-FLIGHT MASS SPECTROMETRY.
Cordeiro FM, Carreira RJ, Rial-Otero R, Rivas MG, Moura I, Capelo JL.
Rapid Commun Mass Spectrom. 2007 Sep 19;21(20):3269-3278 [Epub ahead of print]
305. NMR ASSIGNMENT OF THE APO-FORM OF A Desulfovibrio gigas PROTEIN CONTAINING A NOVEL Mo-Cu CLUSTER
S.R.Pauleta, A.G.Duarte, M.S.Carepo, A.S.Pereira, P.Tavares, I.Moura and J.J.G.Moura
Biomol.NMR Assign (2007) 1, 81-83
306.IMPROVING SAMPLE TREATMENT FOR IN-SOLUTION PROTEIN IDENTIFICATION BY PEPTIDE MASS FINGERPRINT USING MATRIX-ASSISTED LASER DESORPTION/IONIZATION TIME-OF-FLIGHT MASS SPECTROMETRY.
Santos HM, Rial-Otero R, Fernandes L, Vale G, Rivas MG, Moura I, Capelo JL.
Journal of Proteome Research 6 (9), 3393-3399 (2007)
307.SUB-CELLULAR PARTITIONING OF Zn, Cu, Cd AND Pb IN THE DIGESTIVE GLAND OF NATIVE Octopus vulgaris EXPOSED TO DIFFERENT METAL CONCENTRATIONS ( PORTUGAL)
J.Raimundo, C.Vale, R.Duarte and I.Moura
Sci.Total Environ. 390, 416-6 (2008)
308. A NEW TYPE OF METAL-BINDING SITE IN COBALT- AND ZINC-CONTAINING ADENYLATE KINASES ISOLATED FROM SULFATE- REDUCERS D. GIGAS AND D. DESULFURICANS ATCC 27774
Olga Yu. Gavel, Sergey A. Bursakov, Giullia Di Rocco, Alice S. Pereira, Pedro Tavares, Ingrid J. Pickering, Graham N. George, Juan J. Calvete, Jorge Lampreia, José J. G. Moura, and Isabel Moura
J.Inorg.Biochem 102, 1380-1395 (2008)
309. A NEW CATALYTIC MECHANISM OF PERIPLASMIC NITRATE REDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 FROM CRYSTALLOGRAPHIC AND EPR DATA
Shabir Najmudin, Pablo J. González, José Trincão, Catarina Coelho, Abhik Mukhopadhyay, Carlos C. Romão, Isabel Moura, José J. G. Moura, Carlos D. Brondino and Maria J. Romão
J.Biol.Inorg.Chem. 13, 737-753 (2008)
310. INFLUENCE OF THE PROTEIN STAINING IN THE FAST ULTRASONIC SAMPLE
TREATMENT FOR PROTEIN IDENTIFICATION THROUGH PEPTIDE MASS FINGERPRINT AND MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY
Galesio, Marco; Vieira, Diana; Lodeiro, Carlos; Rial-Otero, Raquel; Moura, Isabel; Capelo-Martinez, Jose-Luis
Journal of Proteome Research 7, 2097-2106 (2008)
311. BENEFITS OF MEMBRANE ELECTRODES IN THE ELECTROCHEMISTRY OF METALLOPROTEINS: MEDIATED CATALYSIS OF PARACOCCUS PANTOTROPHUS CYTOCHROME C PEROXIDASE BY HORSE CYTOCHROME C – A CASE STUDY
P. M. Paes de Sousa, S. R. Pauleta, David Rodrigues, M. L. Simões Gonçalves, G. W. Pettigrew, I. Moura, J. J. G. Moura, M. M. Correia dos Santos
J.Biol.Inorg.Chem. 13, 779-787 (2008)
312. CALCIUM-DEPENDENT HEME STRUCTURE IN THE REDUCED FORMS OF THE
BACTERIAL CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS
S.Pauleta, Y.Lu,C.Goodhew,G. Pettigrew, I.Moura,J.Shelnutt
Biochemistry 47, 5841-5850 (2008)
313.PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION ANALYSIS OF THE ADENOSINE TRIPHOSPHATE SULFURYLASE (ATPS) FROM THE SULFATE –REDUCING BACTERIUM Desulfovibrio desulfuricans ATCC 27774
O.Y.Gavel, A.V.Kladova, S.A.Bursakovv, J.M.Dias,S.Teixeira, V.L.Shnyrov, J.J.G.Moura, I.Moura, M.J.Romão and J.Trincão
Acta Crystallogr Sect F Struct Biol Cryst Commun 64,:593-5 (2008)
314. ELECTRON TRANSFER COMPLEX BETWEEN NITROUS OXIDE REDUCTASE (N2OR) AND CYTOCHROME C552 FROM PSEUDOMONAS NAUTICA: KINETIC, NMR AND DOCKING STUDIES
S.Dell’Acqua, S.R.Pauleta, E.Monzani, A.S.Pereira, L.Casella, J.J.G.Moura and I. Moura
Biochemistry 47, 10852–10862 (2008)
315. MODELLING METALLOTHIONEIN INDUCTION IN THE LIVER OF SPARUS AURATA EXPOSED TO METAL-CONTAMINATED SEDIME
Costa PM, Repolho T, Caeiro S, Caeiero, S., Diniz, M.E., Moura, I., Costa, M.H.
Ecotoxicology And Environmental Safety 71, 117-124 (2008)
316. ENZYMATIC ACTIVITY MASTERED BY ALTERING METAL COORDINATION SPHERE
I.Moura, S.R.Pauleta, J.J.G.Moura
J.Biol.Inorg.Chem. 13, 1185-1195 (2008) Aug 22 Epubahead of print
317.DIRECT ELECTROCHEMISTRY OF THE MULTIPLE REDOX CENTERS OF HYDROGENASE D. gigas
I. Moura, C. Cordas and J.J.G. Moura
Bioelectrochemistry 74, 83-89(2008) Ap.26Epubahead of print
318.BIOCHEMICAL AND SPECTROSCOPIC CHARACTERIZATION OF THE MEMBRANE BOUND NITRATE REDUCTASE FROM PSEUDOMONAS NAUTICA 617
Cristina Correia1, Stéphane Besson1,2, Carlos D. Brondino3, Pablo J. González1, Guy Fauque4,5, Jorge Lampreia1, Isabel Moura1 and José J.G. Moura1
J.Biol.Inorg.Chem 13, 1321-33 (2008) Aug 14. [Epub ahead of print]
319. AN IMPROVED CLEAN SONOREACTOR-BASED METHOD FOR PROTEIN IDENTIFICATION BY MASS SPECTROMETRY-BASED TECHNIQUES
Santos HM, Mota C, Lodeiro C, Moura I. , Isaac I, Capelo JL
Talanta 77, 2 , 870-875 (2008)
320. NEW HETEROMETALLIC MO-FE CLUSTER IN A PROTEIN FROM DESULFOVIBRIO ALASKENSIS THAT RESPONDS TO MO-STRESS.
Maria G. Rivas, Marta S. Carepo, Cristiano S. Mota, Malgorzata Korbas, Marie-Claire Durand, Ana T. Lopes, Carlos D. Brondino, Alice Pereira, Graham N. George, Alain Dolla, José J. G. Moura and Isabel Moura
Biochemistry. 48, 873-882 (2009) Jan 14 [Epub ahead of print]
321. CAMELID NANOBODIES RAISED AGAINST AN INTEGRAL MEMBRANE ENZYME, NITRIC OXIDE REDUCTASE
K.Conrath, A. S Pereira; C. Martins,; C. G Timoteo; P. Tavares; S.Spinelli, J. Kinne; C. Flaudrops, C. Cambillau; S. Muyldermans; I. Moura; J. Moura; M. Tegoni,A. Desmyter
Protein Science 18,619-628 (2009) Jan 21[Epub ahead of print]
322. RUBREDOXIN AS A PARAMAGNETIC SHIFT-INDUCING PROBE
R.M.Almeida, S.R.Pauleta, I.Moura and J.J.G.Moura
J.Inorg.Biochem. 103, 1245-53 (2009) [ Epub 2009 Aug 3]
323. ISOLATION AND CHARACTERIZATION OF A NEW CU-FE PROTEIN FROM D.AMINOPHILUS DSM12254
Maria G. Rivas, Cristiano S. Mota, Sofia R. Pauleta, Marta S.P. Carepo, Filipe Folgosa, Susana Andrade, Alice S. Pereira,Pedro Tavares, Juan J. Calvete, Isabel Moura and José J. G. Moura
J.Inorg.Biochem. 103, 1314-1322 (2009) May 7. [Epub ahead of print]
324. KINETIC, STRUCTURAL, AND EPR STUDIES REVEAL THAT ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO GIGAS DOES NOT NEED A SULFIDO LIGAND FOR CATALYSIS AND GIVE EVIDENCE FOR A DIRECT MO-C INTERACTION IN A BIOLOGICAL SYSTEM
T.S.Silva,P.Gonzalez, I.Moura , J.J.G-Moura, M-J-Romão and C.D.Brondino
J.Am.Chem.Soc. 131, 7990-7998(2009) May 21[Epub ahead of print]
325. THE EFFECT OF THE SIXTH SULFUR LIGAND IN THE CATALYTIC MECHANISM OF PERPLASMIC NITRATE REDUCTASE
N.M.F.S.A.Cerqueira, P.J.Gonzalez, C.D.Brondino, M.J.Romão, C.C.Romão, I.Moura, M.J.Ramos and J.J.G.Moura
J Comput Chem. 30, 2466-2484 (2009)Apr 9. [Epub ahead of print]
326.A VARIABLE TEMPERATURE SPECTROSCOPIC STUDY ON P. pantotophus PSEUDOAZURIN: EFFECTS OF PROTEIN CONSTRAINTS ON THE BLUE CU SITE
Xiangjin Xie Ryan G. Hadt, Sofia R. Pauleta, Pablo J. González, Sun Un, Isabel Moura, Edward I. Solomon
J.Inorg.Biochem. 103, 1307-1313 (2009) May 7 [Epub ahead of print]
327.TOTAL LEAD AND ITS STABLE ISOTOPES IN THE DIGESTIVEGLAND OF Octopus vulgaris AS A FINGERPRINT
J.Raimundo , C.Vale, M.Caetano, R.Cesário, I.Moura
Aquat.Biol. 6, 25-30 (2009)
328. CRYSTALLIZATION AND CRYSTALLOGRAPHIC ANALYSIS OF THE APO FORM OF THE ORANGE PROTEIN (ORP) FROM DESULFOVIBRIO GIGAS
S. Najmudin, C. Bonifacio, A. Duarte, S.R.Pauleta, I. Moura, J.J.G. Moura, and M.J. Romão
Acta Crystallogr Sect F Struct Biol Cryst Commun. 65, 926-929 (2009) [Epub 2009 Jun 30]
329 COBALT, ZINC AND IRON FORMS OF ADENYLATE KINASE (AK) FROM THE SULPHATE-REDUCING BACTERIA DESULFOVIBRIO GIGAS: PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION ANALYSIS.
A.V. Kladova, O.Yu. Gavelb, A. Mukhopaadhyay, D.R. Boer, S. Teixeira, V.L. Shnyrov, I. Mouraa, J.J.G. Moura, M.J. Romão, J. Trincão, S.A. Bursakov
Acta Crysta Section F8 (2009) 65, 926-929
330.CAN ULTRASONIC ENERGY EFFICIENTLY SPEED 18O-LABELING OF PROTEINS
R.J.Carreira, C.Lodeiro, M.S.Diniz, I.Moura, J.L.Capelo
Proteomic, 9,4974-7(2009) [ Oct 6 Epub 2009]
331 AN NMR STRUCTURAL STUDY OF NICKEL SUBSTITUTED RUBREDOXIN
Iven Duartea, Anjos L Macedob, José J G Mourab, Brian F Volkmanc, Sofia G Nunesd, I Mourab, John L Markleye, and Brian J Goodfellowa
J.Biol.Inorg.Chem.15,409-420.(2010) Dec 8. [Epub ahead of print]
332. A NEW CuZ ACTIVE FORM IN THE CATALYTIC REDUCTION OF N2O BY NITROUS OXIDE REDUCTASE FROM Pseudomonas nautical
S.Dell’ Acqua, S.R.Pauleta, P.M.P. de Sousa, E. Monzani, L.Casella, J.J.G.Moura and I. Moura
J. Biol.Inorg.Chem. 2010 Apr 27. [Epub ahead of print] 15, 967-76(2010)
333. THE 1.4 Å RESOLUTION STRUCTURE OF Paracoccus pantotrphus PSEUDOAZURIN
S.Najmudin‡, S. R. Pauleta, I. Moura, M. J. Romão
Acta Crysta Section F 66, 627-35(2010) Epub 2010 May 25
334. RUBREDOXIN MUTANT A51C UNFOLDING DYNAMICS: A FÖRSTER RESONANCE
ENERGY TRANSFER STUDY
A. Santos, A.Duarte, I.Moura, J. Martinho and A. Federov
Bioph.Chem. 48, 1313-137 (2010)
335. . METALLOTHIONEINS AND TRACE ELEMENTS IN DIGESTIVE GLAND, GILLS, KIDNEY AND GONADS OF OCTOPUS VULGARIS
J.Raimundo, Costa, P.M., Vale, C., Costa, M.H., Moura, I.
Comparative Biochemistry and Physiology 152, 139-46(2010) 2010 Apr 10. [Epub ahead of print]
336. RELATIONS BETWEEN MERCURY, METHYL-MERCURY AND SELENIUM IN TISSUES OF OCTOPUS VULGARIS FROM THE PORTUGUESE COAST
J. Raimundo, C. Vale, J. Canário, V. Branco, I. Moura.
R. Environmental Pollution 158, 2094-100. Epub 2010 Apr 2.
337. MEASURING THE NITRITE REDUCTASE ACTIVITY-(PRATICAL) CONSIDERATIONS ON THE ENZYME ASSAY
C.M.Silveira, S.Besson, I.Moura, J.J.G.Moura, M.G.Almeida
Bioino. Chem.and Applic.(2010) Epub 2010 June22
338.DNA DAMAGE AND METAL ACUMULATION IN FOUR TISSUES OF FERAL Octopus vulgaris FROM TWO COASTAL AREAS IN PORTUGAL
J.Raimundo, P.M.Costa, C.Vale, M.H.Costa and I.Moura
Ecotoxicol.Environ.Saf. 73, 1543-1547(2010) Aug 16 Epub ahead of print
339. ASSOCIATION OF ZN, CU, CD AND PB WITH PROTEIN FRACTIONS AND SUB-CELLULAR PARTITIONING IN THE DIGESTIVE GLAND OF OCTOPUS VULGARIS LIVING IN HABITATS WITH DIFFERENT METAL LEVELS.
Raimundo J, Vale C, Duarte R, Moura I.
Chemosphere. 10, 1314-1319 (2010) Sep 25. [Epub ahead of print]
340. ARTEFACTS INDUCED ON C-TYPE HAEM PROTEINS BY ELECTRODE SURFACES"
P.M.P. Sousa, S.R. Pauleta, D. Rodrigues, M.L.S. Gonçalves, G.W. Pettigrew,I.Moura, M.M.C. Santos
andJ.J.G. Moura
J. Biol.Inorg.Chem. 16, 209-15 (2011) Epub Oct21(2010)
341. LOW SPIN HEME B3 IN THE CATLYTICAL CENTER OF NITRIC OXIDE REDUCTASE FROM PSEUDOMONAS NAUTICA
C.G.Timóteo, A.S.Pereira, C.E.Martins, S.G.Naik, A.G.Duarte, J.J.G.Moura, P.Tavares, B.H.Huynh and I.Moura
Biochem. 50, 4251-4262 (2011)Mar 31. [Epub ahead of print]
342. CRYSTAL STRUCTURE OF THE ZINC-, COBALT-, AND IRON-CONTAINING ADENYLATE KINASE FROM DESULFOVIBRIO GIGAS: A NOVEL METAL-CONTAINING ADENYLATE KINASE FROM GRAM-NEGATIVE BACTERIA.
Mukhopadhyay A, Kladova AV, Bursakov SA, Gavel OY, Calvete JJ, Shnyrov VL, Moura I, Moura JJ, Romão MJ, Trincão J.
J Biol Inorg Chem. 16, 51-61 (2011) Sep 7 2010 [Epub ahead of print]
343. THE TETRANUCLEAR COPPER ACTIVE SITE OF NITROUS OXIDE REDUCTASE – THE CUZ CENTRE
Dell’Acqua, S.,Pauleta, S.R., Moura, I. and Moura, J.J.G.
J.Biol.Inorg.Chem. 16, 183-94 (2011)
344.THE 1.5A STRUCTURE OF Cupriavidus necator NITRATE REDUCTASE: CRYSTALS OBTAINED WITH IONIC LIQUIDS PROVIDE INSIGHT ON THE PARTILALLY REDUCED CATALYTIC SITE
C.Coelho, P.J.Goz´´alez, J.J.G.Moura, I.Moura, J.Trincão and M.J.Romão
J Mol Biol. 408, 932-48 (21011) Mar 23. [Epub ahead of print]
345. EFFECTS OF MOLYBDATE ON THE GENES EXPRESSION LEVELS AND BIOCHEMICAL CHARACTERISTICS OF FORMATE DEHYDROGENASES PRODUCEDBY Desulfovibrio alaskensis
C.S.Mota, M.C.Durand, P.J.González, C.D.Brondino, J.J.G.Moura, I.Moura, A.Dolla and M.G.Rivas
J. of Bacteriol. 193, 2917-23 (2011) Apr 8. [Epub ahead of print]
346. STRUCTURAL REDOX CONTROL IN A 7FE FERREDOXIN ISOLATED FROM Desulfovibrio alaskensis
Raquel Grazina, Patrícia M. Paes de Sousa, Carlos D. Brondino, Marta S. P. Carepo, Isabel Moura and José J. G. Moura
Bioelectrochemistry. 2011 Apr 28. [Epub ahead of print]
347.ANALYSIS OF THE ACTIVATION MECHANISM OF Pseudomonas stutzeri CYTOCHROME C PEROXIDASE THROUGH AN ELECTRON TRANSFER CHAIN
P.M.Paes de Sousa, D.Rodrigues, C.G.Timóteo, M.L.Simões Gonçalves, G.W.Pettigrew, I.Moura, J.J.G.Moura, M.M.Correia dsos Santos
J.Biol.Inorg.Chem. (2011) May 6. [Epub ahead of print]
348.THE ANAEROBE-SPECIFIC ORP COMPLEX OF Desulfovibrio vulgarisHildenborough IS ENCODED BY TWO DIVERGENT OPERONS CO-REGULATED BY AND COGNATE TRANSCRIPTIONAL REGULATOR
Fiévet, A., My, L., Cascales, E., Ansaldi, M., Pauleta, S., Moura, I., Dermoun, Z., Bernard, C.S., Dolla, A. And Aubert, C.
.J. of Bacteriol. 193, 3207-19 (2011) April 29[Epub ahead of print]
349. THE MECHANISM OF FORMATE OXIDATION BY METAL-DEPENDENT FORMATE DEHYDROGENASES
Mota, C.S., Rivas, M.G., Brondino, C.D., Moura, I., Moura, J.J.G., González, P.J., Cerqueira, N.M.F.S.A.
J. Biol.Inorg. (2011) in press
350. THE ELECTRON TRANSFER COMPLEX BETWEEN NITROUS OXIDE REDUCTASE AND ITS ELECTRON DONORS
S.Dell’Acqua, I.Moura, J.J.G.Moura and S.R.Pauleta
J.Biol.Inorg.Chem (2011) in press
351. NITROUS OXIDE REDUCTASE
S.Dell’Acqua, S.R.Pauleta, I.Moura and J.J.G.Moura
Encyclopedia of Metalloproteins (2011) in press
352. NEW SPECTROSCOPIC AND ELECTROCHEMICALINSIGHTS ON A CLASS I SUPEROXIDE REDUCTASE-EVIDENCE OF AN INTRAMOLECULAR ELECTRN TRANSFER PATHWAY
F.Folgosa, C.M.Cordas, J.A.Santos, A.S.Pereira, J.J.G.Moura, P.Tavares and I.Moura
Biochem.J. (2011) in press
Total de publicações-352 Indice h=49 Total de citações- 8472 Citações por artigo-26.15
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2011-13