J. Moura

发表

Simulation of the electrochemical behavior of multi-redox systems. Current potential studies on multiheme cytochromes.

M. Teixeira, M. I. Montenegro, I. Moura, 1991, European journal of biochemistry.

One electron reduced square planar bis(benzene-1,2-dithiolato) copper dianionic complex and redox switch by O2/HO(-).

J. L. Núñez, L. Maia, A. Rizzi, 2014, Inorganic chemistry.

Proteins containing the factor F430 from methanosarcina barkeri and methanobacterium thermoautotrophicum

H. Santos, I. Moura, H. D. Peck, 1983 .

Purification, characterization and redox properties of hydrogenase from Methanosarcina barkeri (DSM 800).

M. Teixeira, I. Moura, H. D. Peck, 1984, European journal of biochemistry.

Understanding the response of Desulfovibrio desulfuricans ATCC 27774 to the electron acceptors nitrate and sulfate - biosynthetic costs modulate substrate selection.

A. R. Fernandes, B. Devreese, I. Moura, 2017, Biochimica et biophysica acta. Proteins and proteomics.

Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centers and molybdenum)

C. Costa, M. Teixeira, I. Moura, 1997, JBIC Journal of Biological Inorganic Chemistry.

Sulfide and transition metals - A partnership for life.

L. Maia, B. Maiti, J. Moura, 2021, Journal of inorganic biochemistry.

NiII -ATCUN-Catalyzed Tyrosine Nitration in the Presence of Nitrite and Sulfite.

L. Maia, I. Moura, B. Maiti, 2019, Chemistry.

Artefacts induced on c-type haem proteins by electrode surfaces

I. Moura, M. M. Correia dos Santos, S. R. Pauleta, 2011, JBIC Journal of Biological Inorganic Chemistry.

Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway.

A. Wentzel, Giang-Son Nguyen, Malene Jønsson, 2021, Journal of inorganic biochemistry.

Insights into the Molybdenum/Copper Heterometallic Cluster Assembly in the Orange Protein: Probing Intermolecular Interactions with an Artificial Metal-Binding ATCUN Tag.

L. Maia, I. Moura, Rui M Almeida, 2017, Inorganic chemistry.

Perturbation of membrane dynamics in nerve cells as an early event during bilirubin-induced apoptosis.

C. Rodrigues, D. Brites, S. Solá, 2002, Journal of lipid research.

OBSERVATION OF LIGAND-BASED REDOX CHEMISTRY AT THE ACTIVE SITE OF A MOLYBDENUM ENZYME

C. Costa, G. George, I. Moura, 1999 .

Characterization of Desulfovibrio sp. isolated from some lowland paddy field soils of Burkina Faso

A. Lino, I. Moura, A. Traoré, 1998 .

Unusual Reduction Mechanism of Copper in Cysteine-Rich Environment.

J. C. Lima, L. Maia, I. Moura, 2018, Inorganic chemistry.

Electron transfer complex between nitrous oxide reductase and cytochrome c552 from Pseudomonas nautica: kinetic, nuclear magnetic resonance, and docking studies.

E. Monzani, L. Casella, I. Moura, 2008, Biochemistry.

Redox Properties of Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774*

C. Costa, I. Moura, B. Huynh, 1996, The Journal of Biological Chemistry.

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

N. M. Cerqueira, C. Brondino, M. G. Rivas, 2011, JBIC Journal of Biological Inorganic Chemistry.

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

M. Romão, S. Najmudin, N. M. Cerqueira, 2008, JBIC Journal of Biological Inorganic Chemistry.

The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states.

I. Moura, J. Trincao, C. Coelho, 2011, Journal of molecular biology.

Reduction of Carbon Dioxide by a Molybdenum-Containing Formate Dehydrogenase: A Kinetic and Mechanistic Study.

Isabel Moura, L. Maia, I. Moura, 2016, Journal of the American Chemical Society.

Incorporation of a molybdenum atom in a Rubredoxin-type Centre of a de novo-designed α3DIV-L21C three-helical bundle peptide.

V. Pecoraro, I. Moura, S. R. Pauleta, 2022, Journal of Inorganic Biochemistry.

Molybdenum and tungsten-dependent formate dehydrogenases

L. Maia, I. Moura, J. Moura, 2014, JBIC Journal of Biological Inorganic Chemistry.

EPR characterization of the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774 upon formate reduction.

C. Brondino, M. G. Rivas, I. Moura, 2007, Journal of inorganic biochemistry.

Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and the effects of redox poise

R. A. Scott, I. Moura, S. Albracht, 1996 .

Protein-Assisted Formation of Molybdenum Heterometallic Clusters: Evidence for the Formation of S2MoS2-M-S2MoS2 Clusters with M = Fe, Co, Ni, Cu, or Cd within the Orange Protein.

L. Maia, I. Moura, S. R. Pauleta, 2017, Inorganic chemistry.

Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617

C. Brondino, I. Moura, J. Lampreia, 2008, JBIC Journal of Biological Inorganic Chemistry.

Orange protein from Desulfovibrio alaskensis G20: insights into the Mo–Cu cluster protein-assisted synthesis

M. Zakrzewska, I. Moura, A. Dolla, 2016, JBIC Journal of Biological Inorganic Chemistry.

Mo–Cu metal cluster formation and binding in an orange protein isolated from Desulfovibrio gigas

Anthony G. Wedd, Isabel Moura, José J. G. Moura, 2014, JBIC Journal of Biological Inorganic Chemistry.

Synthesis and characterization of [S2MoS2Cu(n-SPhF)]2 −(n = o, m, p) clusters: Potential 19F-NMR structural probes for Orange Protein

I. Moura, S. R. Pauleta, B. Maiti, 2014 .

Membrane structural changes support the involvement of mitochondria in the bile salt-induced apoptosis of rat hepatocytes.

C. Rodrigues, D. Brites, S. Solá, 2002, Clinical science.

Bilirubin directly disrupts membrane lipid polarity and fluidity, protein order, and redox status in rat mitochondria.

C. Rodrigues, D. Brites, S. Solá, 2002, Journal of hepatology.

Tauroursodeoxycholic acid prevents Bax-induced membrane perturbation and cytochrome C release in isolated mitochondria.

C. Steer, C. Rodrigues, S. Solá, 2003, Biochemistry.

Structure and function of ferrochelatase

G. C. Ferreira, J. Moura, I. Moura, 1995, Journal of bioenergetics and biomembranes.

Characterization of the Iron-binding Site in Mammalian Ferrochelatase by Kinetic and Mössbauer Methods (*)

G. C. Ferreira, J. Moura, I. Moura, 1995, The Journal of Biological Chemistry.

ArsC3 from Desulfovibrio alaskensis G20, a cation and sulfate-independent highly efficient arsenate reductase

S. Najmudin, I. Moura, J. Brás, 2014, JBIC Journal of Biological Inorganic Chemistry.

Superoxide Reductase: Different Interaction Modes with its Two Redox Partners

P. Turano, I. Moura, Rui M Almeida, 2013, Chembiochem : a European journal of chemical biology.

The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774. Re-evaluation of the spectroscopic data and redox properties.

Robert Huber, Cristina Costa, Isabel Moura, 2003, European journal of biochemistry.

Revisiting the Catalytic CuZ Cluster of Nitrous Oxide (N2O) Reductase

C Cambillau, T. Haltia, M. Saraste, 2000, The Journal of Biological Chemistry.

Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase

A. Desmyter, S. Muyldermans, C. Cambillau, 2009, Protein science : a publication of the Protein Society.

EPR and Mössbauer Spectroscopic Studies on Enoate Reductase*

M. Teixeira, H. Simon, I. Moura, 1996, The Journal of Biological Chemistry.

A needle in a haystack: The active site of the membrane‐bound complex cytochrome c nitrite reductase

Patrick Bertrand, Isabel Moura, B. Guigliarelli, 2007, FEBS letters.

The Structure of an Electron Transfer Complex Containing a Cytochrome c and a Peroxidase*

C. Costa, I. Moura, C Costa, 1999, The Journal of Biological Chemistry.

A Single Histidine Is Required for Activity of Cytochrome c Peroxidase from Paracoccus denitrificans(*)

B. Devreese, I. Moura, D. Mcginnity, 1996, The Journal of Biological Chemistry.

Mössbauer Characterization of Paracoccus denitrificans Cytochrome c Peroxidase

R. Gilmour, J. Moura, I. Moura, 1995, The Journal of Biological Chemistry.

Control of the spin state of the peroxidatic haem by calcium ions in cytochrome c peroxidase from Paracoccus denitrificans: A 1H NMR study

R. Gilmour, I. Moura, G. Pettigrew, 1993 .

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.

M. Romão, A. Rizzi, C. Brondino, 2009, Journal of the American Chemical Society.

Enzymatic Spectrophotometric Determination of Nitrites in Beer

Cristina Costa, Stefano Girotti, Isabel Moura, 1999 .

Nitric Oxide Reductase: Direct Electrochemistry and Electrocatalytic Activity

J. Moura, I. Moura, Alice S. Pereira, 2006, Chembiochem : a European journal of chemical biology.

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

C. Brondino, J. Moura, M. G. Rivas, 2006, JBIC Journal of Biological Inorganic Chemistry.

Study of the spin-spin interactions between the metal centers of Desulfovibrio gigas aldehyde oxidoreductase: identification of the reducible sites of the [2Fe-2S]1+,2+ clusters.

B. Guigliarelli, P. Bertrand, M. Asso, 2005, Biochemistry.

Isolation and characterization of a rubredoxin and a flavodoxin from Desulfovibrio desulfuricans Berre‐Eau

I. Moura, J. Legall, A. V. Xavier, 1987 .

Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774

R. Huber, C. Costa, M. Romão, 2003, The Journal of Biological Chemistry.

57Fe Q-band pulsed ENDOR of the hetero-dinuclear site of nickel hydrogenase: Comparison of the NiA, NiB, and NiC states

B. Hoffman, I. Moura, A. Pamplona, 1997 .

The solution structure of desulforedoxin, a simple iron-sulfur protein

B. Goodfellow, M. Romão, F. Rusnak, 1996, JBIC Journal of Biological Inorganic Chemistry.

A new CuZ active form in the catalytic reduction of N2O by nitrous oxide reductase from Pseudomonas nautica

E. Monzani, L. Casella, I. Moura, 2010, JBIC Journal of Biological Inorganic Chemistry.

Bacterial nitrate reductases: Molecular and biological aspects of nitrate reduction.

C. Brondino, J. Moura, I. Moura, 2006, Journal of inorganic biochemistry.

Nuclear-magnetic-resonance studies of Desulfuromonas acetoxidans cytochrome c551.5 (c7).

R. J. Williams, G. Moore, I. Probst, 1984, European journal of biochemistry.

Mössbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase.

J. Moura, I. Moura, B. Huynh, 2001, Journal of the American Chemical Society.

Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.

R. A. Scott, J. Moura, I. Moura, 1989, Proceedings of the National Academy of Sciences of the United States of America.

MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association.

D. Nurizzo, C. Cambillau, W. Shepard, 1999, Journal of molecular biology.

Hydrogen metabolism in Desulfovibrio desulfuricans strain New Jersey (NCIMB 8313)--comparative study with D. vulgaris and D. gigas species.

M. Reis, J. Moura, A. Pamplona, 2002, Anaerobe.

Rearrangement of Mo‐Cu‐S Cluster Reflects the Structural Instability of Orange Protein Cofactor

I. Moura, S. R. Pauleta, B. Maiti, 2013 .

Mammalian ferrochelatase, a new addition to the metalloenzyme family.

G. C. Ferreira, J. Moura, I. Moura, 1994, The Journal of biological chemistry.

Hexaheme Nitrite Reductase from Desulfovibrio desulfuricans

C. Costa, Yaning Wang, I. Moura, 1990 .

Nitrate and nitrite utilization in sulfate-reducing bacteria.

C. Costa, J. Moura, I. Moura, 1997, Anaerobe.

Electron transport in sulfate-reducing bacteria. Molecular modeling and NMR studies of the rubredoxin--tetraheme-cytochrome-c3 complex.

P. Weiner, J. Wampler, J. Moura, 1989, European journal of biochemistry.

The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mössbauer characterization.

M. Teixeira, J. Moura, I. Moura, 1990, European journal of biochemistry.

Nickel-[iron-sulfur]-selenium-containing hydrogenases from Desulfovibrio baculatus (DSM 1743). Redox centers and catalytic properties.

M. Teixeira, J. Moura, I. Moura, 1987, European journal of biochemistry.

Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin.

M. Teixeira, J. Moura, I. Moura, 1991, Journal of inorganic biochemistry.

NMR determination of the global structure of the 113Cd derivative of desulforedoxin: Investigation of the hydrogen bonding pattern at the metal center

I. Moura, B. Goodfellow, F. Rusnak, 1998, Protein science : a publication of the Protein Society.

Structural studies by X‐ray diffraction on metal substituted desulforedoxin, a rubredoxin‐type protein

M. Romão, A. Carvalho, M. Archer, 1999, Protein science : a publication of the Protein Society.

A cobalt containing protein isolated from Desulfovibrio gigas, a sulfate reducer.

M. Bruschi, J. Moura, I. Moura, 1980, Biochemical and biophysical research communications.