A5079736054- Metalloenzymes and iron-sulfur proteins
- Metal-Catalyzed Oxygenation Mechanisms
- Photosynthetic Processes and Mechanisms
- Microbial Fuel Cells and Bioremediation
- Electrochemical sensors and biosensors
- Electrocatalysts for Energy Conversion
- Electrochemical Analysis and Applications
- Hemoglobin structure and function
- Enzyme Structure and Function
- Porphyrin Metabolism and Disorders
- Metal complexes synthesis and properties
- Wastewater Treatment and Nitrogen Removal
- Hydrogen Storage and Materials
- Photoreceptor and optogenetics research
- Mass Spectrometry Techniques and Applications
- Spectroscopy and Quantum Chemical Studies
- Redox biology and oxidative stress
- Trace Elements in Health
- Electron Spin Resonance Studies
- Metal Extraction and Bioleaching
- Magnetism in coordination complexes
- Enzyme function and inhibition
- Porphyrin and Phthalocyanine Chemistry
- bioluminescence and chemiluminescence research
- Ammonia Synthesis and Nitrogen Reduction
Universidade Nova de Lisboa
2014-2024
Rede de Química e Tecnologia
2014-2024
Instituto Federal do Amazonas
2024
Unidade em Ciências Biomoleculares Aplicadas
2016
Faculdade de Tecnologia e Ciências
2015
University of Lisbon
1979-2010
Centre National de la Recherche Scientifique
1994-2009
National University of the Littoral
2006-2009
University of Saskatchewan
2009
Universidade de Vigo
2009
The crystal structure of the aldehyde oxido-reductase (Mop) from sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 Å resolution by multiple isomorphous replacement and refined. protein, a homodimer 907 amino acid residues subunits, is member xanthine oxidase family. protein contains molybdopterin cofactor (Mo-co) two different [2Fe-2S] centers. It folded into four domains which first bind iron sulfur centers last are involved in Mo-co binding....
The crystal structure of the xanthine oxidase-related molybdenum-iron protein aldehyde oxido-reductase from sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas (Mop) was analyzed in its desulfo-, sulfo-, oxidized, reduced, and alcohol-bound forms at 1.8-A resolution. In sulfo-form molybdenum molybdopterin cytosine dinucleotide cofactor has a dithiolene-bound fac-[Mo, = O, S, ---(OH2)] substructure. Bound inhibitory isopropanol inner compartment substrate binding tunnel is...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMoessbauer study of D. gigas ferredoxin II and spin-coupling model for Fe3S4 cluster with valence delocalizationV. Papaefthymiou, J. Girerd, I. Moura, G. E. MuenckCite this: Am. Chem. Soc. 1987, 109, 15, 4703–4710Publication Date (Print):July 1, 1987Publication History Published online1 May 2002Published inissue 1 July 1987https://pubs.acs.org/doi/10.1021/ja00249a037https://doi.org/10.1021/ja00249a037research-articleACS PublicationsRequest reuse...
The tetrameric form of a Desulfovibrio gigas ferredoxin, named Fd 11, mediates electron transfer between cytochrome c3 and sulfite reductase.We have studied two stable oxidation states this protein with Mossbauer spectroscopy paramagnetic resonance.We found 3 iron atoms/monomer spin concentration 0.9 spins/monomer for the oxidized protein.Taken together, EPR data demonstrate conclusively presence spin-coupled structure containing atoms labile sulfur.The show also that metal center is...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDetection and characterization of exchangeable protons bound to the hydrogen-activation nickel site Desulfovibrio gigas hydrogenase: a proton deuterium Q-band ENDOR studyChaoliang Fan, Miguel Teixeira, Jose Moura, Isabel Huynh Boi Hanh, Jean Le Gall, Harry D. Peck Jr., Brian M. HoffmanCite this: J. Am. Chem. Soc. 1991, 113, 1, 20–24Publication Date (Print):January 1991Publication History Published online1 May 2002Published inissue 1 January...
The hydrogenase (EC 1.2.2.1) of Desulfovibrio gigas is a complex enzyme containing one nickel center, [3Fe-4S] and two [4Fe-4S] clusters. Redox intermediates this were generated under hydrogen (the natural substrate) using redox-titration technique studied by EPR Mossbauer spectroscopy. In the oxidized states, [4Fe-4S]2+ clusters exhibit broad quadrupole doublet with parameters (apparent delta EQ = 1.10 mm/s 0.35 mm/s) typical for type cluster. Upon reduction, [4Fe-4S]1+ are...
The proton NMR spectra of the tetrahaem cytochrome c 3 from Desulfovibrio gigas were examined while varying pH and redox potential. analysis reoxidation pattern was based on a model for electron distribution between four haems that takes into account haem‐haem interactions. intramolecular exchange is fast time scale (larger than 10 5 s −1 ). data concerning dependence chemical shift haem methyl resonances in different oxidation steps resonance intensities are not compatible with...
Carbon dioxide accumulation is a major concern for the ecosystems, but its abundance and low cost make it an interesting source production of chemical feedstocks fuels. However, thermodynamic kinetic stability carbon molecule makes activation challenging task. Studying chemistry used by nature to functionalize should be helpful development new efficient (bio)catalysts atmospheric utilization. In this work, ability Desulfovibrio desulfuricans formate dehydrogenase (Dd FDH) reduce was...
Nitrous-oxide reductases (N2OR) catalyze the two-electron reduction of N<sub>2</sub>O to N<sub>2</sub>. The crystal structure N2ORs from <i>Pseudomonas nautica</i>(Pn) and <i>Paracoccus denitrificans</i> (Pd) were solved at resolutions 2.4 1.6 Å, respectively. Pn N2OR revealed that catalytic CuZ center belongs a new type metal cluster in which four copper ions are liganded by seven histidine residues. A bridging oxygen moiety two other hydroxide ligands proposed complete ligation scheme...
The periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenbourough) is an all Fe-containing hydrogenase. It contains two ferredoxin type [4Fe-4S] clusters, termed the F and a catalytic H cluster. Recent X-ray crystallographic studies on Fe hydrogenases revealed that cluster composed sub-clusters, ([4Fe-4S](H)) binuclear ([2Fe](H)), bridged by cysteine sulfur. aerobically purified D. stable in air. inactive requires reductive activation. Upon reduction, enzyme becomes sensitive to O(2),...
Desulfovibrio gigas hydrogenase (EC 1.12.2.1) is a complex enzyme containing one nickel, 3Fe, and two [Fe4S4] clusters (Teixeira, M., Moura, I., Xavier, A. V., Der Vartanian, D. LeGall, J., Peck, H. D., Jr., Huynh, B. H., J. G. (1983) Eur. Biochem. 130, 481-484). This belongs to class of enzymes that are inactive as isolated (the so-called oxygen-stable hydrogenases) must go through an activation process in order express full activity. The state characterization the active centers prompted...
The hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified each of three different fractions: soluble periplasmic (wash), cytoplasmic (cell disruption) and membrane‐bound (detergent solubilization). Plasma‐emission metal analysis detected in all fractions the presence iron plus nickel selenium equimolecular amounts. These hydrogenases were shown to be composed two non‐identical subunits distinct with respect their spectroscopic properties. EPR spectra native (as isolated) enzymes...