jjgm

José João Galhardas de Moura
Full Professor
Integrated Member
Research Group
Structural Molecular Biology
Department of Chemistry, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal
212 948 382
- ext 10932
212 948 550
Research Interests
KEY WORDS
Bioinorganic, Biophysics, Biocatalysis, Energy Bioconversion (Hydrogen), Role of metals in Biology (heme and non-heme iron, molybdenum, tungsten, nickel, copper, vanadium and cobalt), Inorganic systems as models for biocatalysis, Spectroscopy (NMR, EPR and Mössbauer), (Bio) Electrochemistry, Protein-Protein interactions.

Main goal is the understanding of electron transfer chains (ETC) of sulphate reducing bacteria (SRB) and methane forming bacteria (MFB). SRB have complex ETC systems which allow the reduction of sulphate by oxidation of either organic compounds or molecular hydrogen. The result of the bacterial activity results in the formation of large amounts of sulphide which presents serious health and environmental problems (metal corrosion, poisoning, etc). Another interest of these microorganisms is due to the fact that can either use or produce molecular hydrogen. In this last case, hydrogen is oxidized by other microbial groups (MFB) producing methane by reduction of carbon dioxide. The understanding of the involved mechanisms is important to study the use of new forms of energy (bioconversion - biological production of hydrogen and methane). A necessary step is the identification and isolation of metalloenzymes involved. The main goal is the use of spectroscopic techniques namely electron paramagnetic resonance (RPE) and related methods (ENDOR and ESEEM), uni- and multi-dimensional nuclear magnetic resonance RMN) and Mossbauer spectroscopy on the study of structure-function relationship of metallo-proteins and reconstitution of electron transfer chains (protein/protein interactions using Molecular graphics). The active centers that have been studied include iron-sulphur clusters (rubredoxin type, [2Fe -2S], [3Fe-4S], [4Fe-4S] and novel Fe-S centers), as well as associations with molybdenum and nickel) and hemes. Special relevance has been given to the characterization of bacterial hydrogenases (the role of the nickel in hydrogen evolution/ consumption) and to the topics: engineering of iron-sulphur proteins, chemical modification of active centers, synthesis of novel metal clusters (formation of clusters containing hetero-atoms) and molecular modeling.

Research highlights:

Discovery of a novel 3Fe center and Heterometallic Fe-S sites
Isolation of novel Metalloproteins
Role of Nickel in Hydrogenases
Role of Molybdenum (and Tungsten) in Biology
Electron Transfer and Protein-Protein Interactions in Metalloproteins
Main publications
see
http://docentes.fct.unl.pt/jjgm

a few recent publications

Induced peroxidase activity of haem containing nitrate reductases revealed by protein film electrochemistry
Catarina Coelho, Jacopo Marangon, David Rodrigues, José J.G. Moura, Maria João Romão,
Patrícia M. Paes de Sousa, Margarida M. Correia dos Santos
Journal of Electroanalytical Chemistry 693 (2013) 105–113.

Insights into the electrochemical behaviour of composite materials: Monovacant polyoxometalates porous metal-organic framework
Patrícia M. Paes de Sousa, Raquel Grazina, André D.S. Barbosa, Baltazar de Castro, José J.G. Moura, Luís Cunha-Silva, Salete S. Balula
Electrochimica Acta 87 (2013) 853– 859.

Periplasm Nitrate reductases and Formate dehydrogenases: Control of the Chemical Properties of Mo and W for Fine Tuning of Reactivity and Substrate Specificity
Pablo J. Gonzalez, Maria G. Rivas, Cristiano S. Mota, Carlos D. Brondino, Isabel Moura, José J. G. Moura
Coordination Chemical Reviews CCR (2013) 2, 315-331.
DOI:10.1016/j.ccr.2012.05.020
65th Birthday celebration issue for Ed Solomon.

Rearrangement of Mo-Cu-S Cluster Reflects the Structural Instability of Orange Protein Cofactor
Biplab K. Maiti, Teresa Avilés, Marta S. P. Carepo, Isabel Moura, Sofia R. Pauleta and José J. G. Moura
ZAAC - Zeitschrift für Anorganische und Allgemeine Chemie (2013)
DOI: 10.1002/zaac.20130034

Copper-substituted forms of the wild type and C42A variant of rubredoxin
A.Thapper, A.C.Rizzi, C.D.Brondino, A.G.Wedd, R.J.Pais, I.Moura, S.R.Pauleta and J.J.G.Moura
J Inorg Biochem. 2013 Jun 13.
doi: 10.1016/j.jinorgbio.2013.06.003.

Superoxide reductase: different interaction modes with its two redox partners.
Rui M. Almeida, Paola Turano, Isabel Moura, José J. G. Moura, Sofia R. Pauleta.
ChemBioChem (2013). In Press. DOI: 10.1002/cbic.201300196.

Nitrous oxide reductase.
Simmone Dell'acqua, Sofia R. Pauleta**, Isabel Moura, José J. G. Moura.
Encyclopedia of Metalloproteins. (2013)
Eds. R.H. Kretsinger, V. N. Uversky, E.A. Permyakov.
Springer. ISBN: 978-1-4614-1532-9.

Iron–Sulfur Centers: New Roles for Ancient Metal Sites. Grazina R., Pauleta S.R., Moura J.J.G. and Moura I.
In: Jan Reedijk and Kenneth Poeppelmeier, editors. Comprehensive Inorganic
Chemistry II, Vol 3. Oxford: Elsevier; 2013. p. 103-148.

Electrochemical behaviour of bacterial nitric oxide reductase-evidence of low redox potential non-heme Fe(B) gives new perspectives on the catalytic mechanism.
Cristina M. Cordas, Américo G. Duarte, José J. G. Moura, Isabel Moura I.
Biochim Biophys Acta (2013) 1827(3):233-8
doi: 10.1016/j.bbabio.2012.10.018.