S. R. Pauleta

发表

Predicting Protein-Protein Interactions Using BiGGER: Case Studies

Ludwig Krippahl, José J. G. Moura, L. Krippahl, 2016, Molecules.

Rubredoxin as a paramagnetic relaxation-inducing probe.

J. Moura, I. Moura, Rui M Almeida, 2009, Journal of inorganic biochemistry.

A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase.

F. Guerlesquin, S. Harding, J. Moura, 2004, Biochemistry.

Mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by P. pantotrophus pseudoazurin: kinetics of intermolecular electron transfer

I. Moura, M. M. Correia dos Santos, S. R. Pauleta, 2007, JBIC Journal of Biological Inorganic Chemistry.

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.

NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a novel Mo–Cu cluster

J. Moura, I. Moura, Alice S. Pereira, 2007, Biomolecular NMR assignments.

Acrylamide-hemoglobin adduct: A spectroscopic study.

S. R. Pauleta, André G Favinha, Daniela S. Barreiro, 2020, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases

J. Moura, I. Moura, P. Tavares, 2006, JBIC Journal of Biological Inorganic Chemistry.

Pressure perturbation calorimetry and the thermodynamics of noncovalent interactions in water: comparison of protein-protein, protein-ligand, and cyclodextrin-adamantane complexes.

A. Cooper, S. R. Pauleta, G. Pettigrew, 2010, The journal of physical chemistry. B.

A variable temperature spectroscopic study on Paracoccuspantotrophus pseudoazurin: protein constraints on the blue Cu site.

E. Solomon, Ryan G. Hadt, I. Moura, 2009, Journal of inorganic biochemistry.

Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus.

J. Moura, I. Moura, Rui M Almeida, 2017, Journal of inorganic biochemistry.

Nitrous oxide reductase

I. Moura, S. Dell'Acqua, S. R. Pauleta, 2013 .

The effect of pH on Marinobacter hydrocarbonoclasticus denitrification pathway and nitrous oxide reductase

I. Moura, S. R. Pauleta, O. Mestre, 2020, JBIC Journal of Biological Inorganic Chemistry.

Analysis of resonance Raman data on the blue copper site in pseudoazurin: excited state π and σ charge transfer distortions and their relation to ground state reorganization energy.

E. Solomon, Ryan G. Hadt, I. Moura, 2012, Journal of inorganic biochemistry.

The catalytic cycle of nitrous oxide reductase - The enzyme that catalyzes the last step of denitrification.

I. Moura, S. R. Pauleta, C. Carreira, 2017, Journal of inorganic biochemistry.

Spectroscopic Definition of the CuZ° Intermediate in Turnover of Nitrous Oxide Reductase and Molecular Insight into the Catalytic Mechanism.

E. Solomon, I. Moura, S. Dell'Acqua, 2017, Journal of the American Chemical Society.

Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase: redox dependence and insight into reactivity

E. Solomon, I. Moura, S. Dell'Acqua, 2015, Chemical science.

Determination of the active form of the tetranuclear copper sulfur cluster in nitrous oxide reductase.

E. Solomon, I. Moura, S. R. Pauleta, 2014, Journal of the American Chemical Society.

Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase.

J. V. Van Beeumen, B. Devreese, F. Guerlesquin, 2004, Biochemistry.

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.

Enzymatic activity mastered by altering metal coordination spheres

J. Moura, I. Moura, S. R. Pauleta, 2008, JBIC Journal of Biological Inorganic Chemistry.

The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

J. Moura, I. Moura, S. Dell'Acqua, 2011, JBIC Journal of Biological Inorganic Chemistry.

Calcium-dependent heme structure in the reduced forms of the bacterial cytochrome c peroxidase from Paracoccus pantotrophus.

J. Shelnutt, I. Moura, S. R. Pauleta, 2008, Biochemistry.

Photomodulation of ultrastable host–guest complexes in water and their application in light-controlled steroid release

Paulo J. Costa, U. Pischel, N. Basílio, 2022, Organic Chemistry Frontiers.

Incorporation of molybdenum in rubredoxin: models for mononuclear molybdenum enzymes

L. Maia, J. Moura, I. Moura, 2015, JBIC Journal of Biological 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.

Copper-substituted forms of the wild type and C42A variant of rubredoxin.

A. Rizzi, C. Brondino, J. Moura, 2013, Journal of inorganic biochemistry.

The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase.

B. Devreese, S. R. Pauleta, I. H. Saraiva, 2016, Biochimica et biophysica acta.

Source and reduction of nitrous oxide

I. Moura, S. R. Pauleta, M. Carepo, 2019, Coordination Chemistry Reviews.

The small iron-sulfur protein from the ORP operon binds a [2Fe-2S] cluster.

J. Moura, I. Moura, S. R. Pauleta, 2016, Biochimica et Biophysica Acta.

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.

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.

Genomic organization, gene expression and activity profile of Marinobacter hydrocarbonoclasticus denitrification enzymes

I. Moura, S. R. Pauleta, O. Mestre, 2018, PeerJ.

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

J. Moura, I. Moura, A. G. Wedd, 2014, JBIC Journal of Biological Inorganic Chemistry.

Iron-Sulfur Centers: New Roles for Ancient Metal Sites

J. Moura, I. Moura, S. R. Pauleta, 2013 .

The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis

C. Brochier-Armanet, B. Py, Z. Dermoun, 2019, Scientific Reports.

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.

The Anaerobe-Specific Orange Protein Complex of Desulfovibrio vulgaris Hildenborough Is Encoded by Two Divergent Operons Coregulated by σ54 and a Cognate Transcriptional Regulator

E. Cascales, M. Ansaldi, I. Moura, 2011, Journal of bacteriology.

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.

S. R. Pauleta, A. Echalier, G. Pettigrew, 2006, Journal of inorganic biochemistry.

Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase

J. Moura, I. Moura, S. Dell'Acqua, 2012, Philosophical Transactions of the Royal Society B: Biological Sciences.

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

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

Gd(III) chelates as NMR probes of protein-protein interactions. Case study: rubredoxin and cytochrome c3.

C. Geraldes, J. Moura, Rui M Almeida, 2011, 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 .

Reduction of hydrogen peroxide in gram-negative bacteria - bacterial peroxidases.

S. R. Pauleta, C. Nóbrega, 2019, Advances in microbial physiology.

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.

Isolation and characterization of a new Cu-Fe protein from Desulfovibrio aminophilus DSM12254.

J. Calvete, S. Andrade, J. Moura, 2009, Journal of inorganic biochemistry.

YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity.

B. Devreese, S. R. Pauleta, C. Nóbrega, 2018, Biochimica et biophysica acta. Bioenergetics.

Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus - An electrochemical study.

I. Moura, S. R. Pauleta, C. Carreira, 2020, Bioelectrochemistry.

The electron transfer complex between nitrous oxide reductase and its electron donors

J. Moura, I. Moura, S. Dell'Acqua, 2011, JBIC Journal of Biological Inorganic Chemistry.

Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study

I. Moura, M. M. Correia dos Santos, S. R. Pauleta, 2008, JBIC Journal of Biological Inorganic Chemistry.

OrpR is a σ54‐dependent activator using an iron‐sulfur cluster for redox sensing in Desulfovibrio vulgaris Hildenborough

E. Biondi, G. Brasseur, Z. Dermoun, 2021, Molecular microbiology.

Bacterial peroxidases – Multivalent enzymes that enable the use of hydrogen peroxide for microaerobic and anaerobic proliferation

S. R. Pauleta, Daniela S. Barreiro, R. N. Oliveira, 2023, Coordination Chemistry Reviews.

Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase—Insights into the Catalytic Cycle of Bacterial Peroxidases

M. Romão, A. Carvalho, S. R. Pauleta, 2023, International journal of molecular sciences.

Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae.

B. Devreese, S. R. Pauleta, G. van Driessche, 2017, Journal of inorganic biochemistry.

Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function

C. Donadoni, L. Banci, Lei Hu, 2014, Proceedings of the National Academy of Sciences.

1H, 13C and 15N resonance assignment of the soluble form of the Lipid-modified Azurin from Neisseriagonorrhoeae

S. R. Pauleta, M. Matzapetakis, C. Nóbrega, 2013, Biomolecular NMR assignments.

1H, 13C and 15N resonance assignment of the soluble form of the Lipid-modified Azurin from Neisseriagonorrhoeae

S. R. Pauleta, M. Matzapetakis, C. Nóbrega, 2012, Biomolecular NMR Assignments.

The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis

C. Brochier-Armanet, B. Py, Z. Dermoun, 2019, Scientific Reports.

Biochemical characterization of AniA from Neisseria gonorrhoeae

S. R. Pauleta, Daniela S. Barreiro, R. N. Oliveira, 2022, bioRxiv.

Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid‐modified azurin

S. R. Pauleta, C. Nóbrega, 2018, FEBS letters.

The 1.4 A resolution structure of Paracoccus pantotrophus pseudoazurin.

M. Romão, S. Najmudin, I. Moura, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

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.

Resonance assignment of DVU2108 that is part of the Orange Protein complex in Desulfovibrio vulgaris Hildenborough

S. R. Pauleta, M. Carepo, Rui Soares, 2016, Biomolecular NMR assignments.

Resonance assignment of DVU2108 that is part of the Orange Protein complex in Desulfovibrio vulgaris Hildenborough

S. R. Pauleta, M. Carepo, Rui Soares, 2015, Biomolecular NMR Assignments.

Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas.

M. Romão, S. Najmudin, J. Moura, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structural changes associated with calcium-dependent activation of the di-heme cytochrome c peroxidase of Paracoccus pantotrophus

J. Shelnutt, Y. Lu, I. Moura, 2001 .

Cytochrome c peroxidase and its redox partners - binary and ternary complexes

C. Costa, L. Krippahl, S. Harding, 2001 .

Coordination of the N-Terminal Heme in the Non-Classical Peroxidase from Escherichia coli

S. R. Pauleta, R. N. Oliveira, Sara R M M de Aguiar, 2023, Molecules.

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

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