R. Coelho

ORCID: 0009-0009-7580-8438
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About
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Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • Hydrogen Storage and Materials
  • Electrocatalysts for Energy Conversion
  • Enzyme Production and Characterization
  • Enzyme Structure and Function
  • Estrogen and related hormone effects
  • Catalysis and Hydrodesulfurization Studies
  • Porphyrin Metabolism and Disorders
  • Polysaccharides and Plant Cell Walls
  • Porphyrin and Phthalocyanine Chemistry
  • Biofuel production and bioconversion
  • Photosynthetic Processes and Mechanisms
  • Radioactive element chemistry and processing
  • Prostate Cancer Treatment and Research
  • Microbial Metabolites in Food Biotechnology
  • Hormonal and reproductive studies
  • Microbial Fuel Cells and Bioremediation
  • Metal-Catalyzed Oxygenation Mechanisms
  • Metal Extraction and Bioleaching
  • Fungal Biology and Applications
  • ATP Synthase and ATPases Research
  • Origins and Evolution of Life
  • Hemoglobin structure and function
  • Metal complexes synthesis and properties
  • Vitamin K Research Studies

Centro Universitário Cesumar
2024

Universidade Federal de Minas Gerais
2022

Universidade Nova de Lisboa
2000-2013

Instituto de Biologia Molecular e Celular
2004

Institut de génétique et de biologie moléculaire et cellulaire
2000

Inserm
2000

Instituto de Biologia Experimental e Tecnológica
1998-2000

University of Groningen
2000

Instituto Português Da Qualidade
1998

Pfizer (United Kingdom)
1996

The crystal structures of the human androgen receptor (hAR) and progesterone ligand-binding domains in complex with same ligand metribolone (R1881) have been determined. Both three-dimensional show typical nuclear fold. change two residues pocket between hAR is most likely source for specificity R1881 to hAR. structural implications 14 known mutations associated either prostate cancer or partial complete insensitivity syndrome were analyzed. effects these mutants could be explained on basis...

10.1074/jbc.m004571200 article EN cc-by Journal of Biological Chemistry 2000-08-01

The crystal structure of wild-type endo-β-D-1,4-mannanase (EC 3.2.1.78) from the ascomycete Chrysonilia sitophila (CsMan5) has been solved at 1.40 Å resolution. enzyme isolated directly source shows mixed activity as both an endo-glucanase and endo-mannanase. CsMan5 adopts (β/α) 8 -barrel fold that is well conserved within GH5 family highest sequence structural homology to endo-mannanases. Superimposition with proteins this a unique arrangement three surface loops stretch over active centre,...

10.1107/s0907444912034646 article EN Acta Crystallographica Section D Biological Crystallography 2012-10-18

Detailed structural models of di‐cluster seven‐iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors’ role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 Å resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by N‐terminal extension comprising His/Asp Zn 2+ site ferredoxin (βαβ) 2 core, which harbours intact clusters I II,...

10.1016/j.febslet.2008.01.041 article EN FEBS Letters 2008-02-05

RNA degradation is important in the post-transcriptional control of gene expression. The processing, and quality performed by many different classes ribonucleases. Ribonuclease II (RNase II) a 643-amino-acid enzyme that degrades single-stranded from its 3′-­end, releasing ribonucleoside 5′-monophosphates. RNase was expressed both as wild type D209N mutant form. latter also produced an SeMet derivative. various protein forms were crystallized using vapour-diffusion method. Wild-type two...

10.1107/s1744309106021506 article EN Acta Crystallographica Section F Structural Biology and Crystallization Communications 2006-06-26

The [NiFeSe] hydrogenases belong to a subgroup of the [NiFe] proteins in which selenocysteine is ligand Ni. These enzymes demonstrate interesting catalytic properties, showing very high H2-producing activity that sustained presence low O2 concentrations. purification, crystallization and preliminary X-ray diffraction analysis hydrogenase isolated from Desulfovibrio vulgaris Hildenborough are reported. Crystals soluble form this were obtained using 20% PEG 1500 as precipitant belonged...

10.1107/s1744309109031261 article EN Acta Crystallographica Section F Structural Biology and Crystallization Communications 2009-08-21

Este artigo tem como objetivo a análise dos atuais critérios diagnósticos para sensibilidade ao glúten não celíaca (SGNC), visto que ainda há um protocolo bem definido investigação desta condição clínica, pautando apenas na exclusão de outras patologias doença e alergia trigo. Foram utilizados descritores busca as seguintes palavras: hipersensibilidade trigo, diarreia, dor abdominal, dieta livre glúten. aplicados os operadores booleanos AND OR, nos bancos dados: Scielo PubMed. Por fim, foram...

10.36557/2674-8169.2024v6n5p196-213 article PT cc-by Brazilian Journal of Implantology and Health Sciences 2024-05-03

RuvBL1, an evolutionary highly conserved protein related to the AAA+ family of ATPases, has been crystallized using hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong space group P6, with unit-cell parameters a = b 207.1, c 60.7 Å three molecules in asymmetric unit.

10.1107/s1744309105041400 article EN Acta Crystallographica Section F Structural Biology and Crystallization Communications 2005-12-16

Crystals of rubredoxin oxygen oxidoreductase have been obtained and characterized. They belong to space group P 2 1 2, with unit-cell dimensions a = 88.24 (15), b 101.25 (7), c 90.80 (3) Å. The homodimer (86 kDa) in the asymmetric unit is related by non-crystallographic twofold rotation axis parallel ab `diagonal' direction, as shown self-rotation maximum section χ 180°. This pseudo-crystallographic symmetry element was also found be twinning pseudo-merohedrally twinned crystals, leading...

10.1107/s0907444999006216 article EN Acta Crystallographica Section D Biological Crystallography 1999-08-01

The plant aspartic proteinase cardosin A was crystallized using vapour diffusion. Crystals belong to the monoclinic space group C2, cell dimensions a = 116.9 (2), b 87.2 (8), c 81.3 (1) Å, β 104.4 (4)°, and contain two molecules in asymmetric unit related by non-crystallographic twofold axis. Diffraction data were collected at room temperature with radiation from synchrotron source up 2.85 Å resolution. When crystals flash cooled 110 K nitrogen stream same resolution limit could also be...

10.1107/s0907444998001048 article EN Acta Crystallographica Section D Biological Crystallography 1998-09-01
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