José J. G. Moura

Research interests

Publications

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

  Journal of the American Chemical Society · 2016 · https://doi.org/10.1021/jacs.6b03941

• Molybdenum and tungsten-containing formate dehydrogenases: Aiming to inspire a catalyst for carbon dioxide utilization

  Inorganica Chimica Acta · 2016 · https://doi.org/10.1016/j.ica.2016.07.010

• Molybdenum and tungsten-dependent formate dehydrogenases

  JBIC Journal of Biological Inorganic Chemistry · 2014 · https://doi.org/10.1007/s00775-014-1218-2

• How Biology Handles Nitrite

  Chemical Reviews · 2014 · https://doi.org/10.1021/cr400518y

• Metalloenzymes of the denitrification pathway

  Journal of Inorganic Biochemistry · 2006 · 10.1016/j.jinorgbio.2006.09.003

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

  Journal of Inorganic Biochemistry · 2006 · 10.1016/j.jinorgbio.2005.11.024

• Chemical composition and pulping of banana pseudo-stems

  Industrial Crops and Products · 2003 · 10.1016/j.indcrop.2003.09.001

• Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas

  Structure · 2002 · https://doi.org/10.1016/s0969-2126(02)00826-2

• 17O ENDOR Detection of a Solvent-Derived Ni−(OHx)−Fe Bridge That Is Lost upon Activation of the Hydrogenase fromDesulfovibrio gigas

  Journal of the American Chemical Society · 2001 · https://doi.org/10.1021/ja010204v

• Mössbauer Characterization of the Iron−Sulfur Clusters in Desulfovibrio vulgaris Hydrogenase

  Journal of the American Chemical Society · 2001 · https://doi.org/10.1021/ja003176+

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

  Journal of Biological Chemistry · 2000 · https://doi.org/10.1074/jbc.m008617200

• BiGGER: A new (soft) docking algorithm for predicting protein interactions

  Proteins Structure Function and Bioinformatics · 2000 · https://doi.org/10.1002/(sici)1097-0134(20000601)39:4<372::aid-prot100>3.0.co;2-q

• A novel type of catalytic copper cluster in nitrous oxide reductase.

  Nature Structural Biology · 2000 · https://doi.org/10.1038/73288

• Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods

  Structure · 1999 · 10.1016/s0969-2126(99)80010-0

• A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.

  Proceedings of the National Academy of Sciences · 1996 · 10.1073/pnas.93.17.8846

• Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas

  Science · 1995 · https://doi.org/10.1126/science.270.5239.1170

• Detection and characterization of exchangeable protons bound to the hydrogen-activation nickel site of Desulfovibrio gigas hydrogenase: a proton and deuterium Q-band ENDOR study

  Journal of the American Chemical Society · 1991 · https://doi.org/10.1021/ja00001a003

• Redox Intermediates of Desulfovibrio gigas [NiFe] Hydrogenase Generated Under Hydrogen

  Journal of Biological Chemistry · 1989 · https://doi.org/10.1016/s0021-9258(19)84725-7

• EPR studies with 77Se-enriched (NiFeSe) hydrogenase of Desulfovibrio baculatus

  Journal of Biological Chemistry · 1989 · https://doi.org/10.1016/s0021-9258(19)81667-8

• The three classes of hydrogenases from sulfate-reducing bacteria of the genusDesulfovibrio

  FEMS Microbiology Letters · 1988 · 10.1111/j.1574-6968.1988.tb02748.x

• Nickel‐[iron‐sulfur]‐selenium‐containing hydrogenases from Desulfovibrio baculatus (DSM 1743)

  European Journal of Biochemistry · 1987 · https://doi.org/10.1111/j.1432-1033.1987.tb13302.x

• Moessbauer study of D. gigas ferredoxin II and spin-coupling model for Fe3S4 cluster with valence delocalization

  Journal of the American Chemical Society · 1987 · 10.1021/ja00249a037

• Electron paramagnetic resonance studies on the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from Desulfovibrio gigas.

  Journal of Biological Chemistry · 1985 · https://doi.org/10.1016/s0021-9258(17)39440-1

• NMR studies of electron transfer mechanisms in a protein with interacting redox centres: Desulfovibrio gigas cytochrome c3

  European Journal of Biochemistry · 1984 · https://doi.org/10.1111/j.1432-1033.1984.tb08190.x

• The presence of redox-sensitive nickel in the periplasmic hydrogenase from Desulfovibriogigas

  Biochemical and Biophysical Research Communications · 1982 · https://doi.org/10.1016/0006-291x(82)91154-8

• Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mössbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II.

  Journal of Biological Chemistry · 1982 · https://doi.org/10.1016/s0021-9258(20)65132-8

• Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies.

  Journal of Biological Chemistry · 1980 · 10.1016/s0021-9258(19)85685-5

Current projects

No projects listed.