Inês A. C. Pereira

ORCID: 0000-0003-3283-4520
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About
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Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • Electrocatalysts for Energy Conversion
  • Microbial Fuel Cells and Bioremediation
  • Hydrogen Storage and Materials
  • CO2 Reduction Techniques and Catalysts
  • Microbial Community Ecology and Physiology
  • Advanced Photocatalysis Techniques
  • Advanced battery technologies research
  • Photosynthetic Processes and Mechanisms
  • Enzyme Structure and Function
  • Anaerobic Digestion and Biogas Production
  • Mine drainage and remediation techniques
  • Electrochemical sensors and biosensors
  • Metal-Catalyzed Oxygenation Mechanisms
  • Genomics and Phylogenetic Studies
  • Cassava research and cyanide
  • Enzyme Catalysis and Immobilization
  • Biochemical and Molecular Research
  • Electrochemical Analysis and Applications
  • Nitrogen and Sulfur Effects on Brassica
  • Porphyrin Metabolism and Disorders
  • Metal Extraction and Bioleaching
  • Hemoglobin structure and function
  • Methane Hydrates and Related Phenomena
  • Catalysis for Biomass Conversion

Universidade Nova de Lisboa
2016-2025

Instituto de Tecnología Química
2000-2025

Bioénergétique et Ingénierie des Protéines
2023

Centre National de la Recherche Scientifique
2000-2023

Instituto de Biologia Experimental e Tecnológica
2005-2023

University of Lisbon
2022-2023

Aix-Marseille Université
2023

Hospital CUF Descobertas
2023

Instituto de Engenharia de Sistemas e Computadores Investigação e Desenvolvimento
2023

Instituto Politécnico de Leiria
2023

The number of sequenced genomes sulfate reducing organisms (SRO) has increased significantly in the recent years, providing an opportunity for a broader perspective into their energy metabolism. In this work we carried out comparative survey metabolism genes found 25 available SRO. This analysis revealed higher diversity possible conserving pathways than classically considered to be present these organisms, and permitted identification new proteins not known group. Deltaproteobacteria (and...

10.3389/fmicb.2011.00069 article EN cc-by Frontiers in Microbiology 2011-01-01

Sulfate reduction via a trisulfide Microorganisms can respire sulfur compounds in the absence of oxygen, eventually leading to production hydrogen sulfide. This ancient metabolism is common modern anoxic environments, but enzymatic pathways aren't yet fully resolved. Through vivo and vitro experiments, Santos et al. clarify enzymology sulfate pathway both bacteria archaea (see Perspective by Fritz Kroneck). Reduction sulfite intermediate results linkage two cysteine residues third atom from...

10.1126/science.aad3558 article EN Science 2015-12-17

Fuel-forming enzymes can display excellent performance, achieving high rates of catalysis with unity selectivity at minimal overpotentials, but they are generally considered to be fragile and difficult handle in combination synthetic semiconductors light-driven chemical synthesis. Here, we demonstrate a biohybrid platform that is assembled from cyanamide-functionalized carbon nitride (CNX) as scalable inexpensive photosensitizer selectively photo-oxidizes 4-methyl benzyl alcohol (MBA) its...

10.1021/jacs.4c10519 article EN cc-by Journal of the American Chemical Society 2025-02-28

We have searched for sulfate-reducing bacteria in the feces of 41 healthy individuals and 110 patients from a Hepato-Gastro-Enterology Unit using specific liquid medium (Test-kit Labège, Compagnie Française de Géothermie, Orléans, France). The were separated 22 presenting with inflammatory bowel diseases 88 hospitalized other lower (n=30) or upper (n=58) digestive tract diseases. Sulfate-reducing isolated 10 (24%), 15 (68%), 33 symptoms (37%). A multiplex PCR was devised identification...

10.1111/j.1574-6941.2002.tb00942.x article EN FEMS Microbiology Ecology 2002-05-01

Sulfate reduction is one of the earliest types energy metabolism used by ancestral organisms to sustain life. Despite extensive studies, many questions remain about way respiratory sulfate associated with conservation. A crucial enzyme in this process dissimilatory sulfite reductase (dSiR), which contains a unique siroheme-[4Fe4S] coupled cofactor. Here, we report structure desulfoviridin from Desulfovibrio vulgaris, dSiR DsrAB (sulfite reductase) subunits are bound DsrC protein. The...

10.1074/jbc.m805643200 article EN cc-by Journal of Biological Chemistry 2008-10-02

Summary Desulfatibacillum alkenivorans AK‐01 serves as a model organism for anaerobic alkane biodegradation because of its distinctive biochemistry and metabolic versatility. The D. genome provides blueprint understanding the genetic systems involved in metabolism including substrate activation, CoA ligation, carbon‐skeleton rearrangement decarboxylation. Genomic analysis suggested route to regenerate fumarate needed activation via methylmalonyl‐CoA predicted capability syntrophic...

10.1111/j.1462-2920.2011.02516.x article EN Environmental Microbiology 2011-06-08

The integration of enzymes with synthetic materials allows efficient electrocatalysis and production solar fuels. Here, we couple formate dehydrogenase (FDH) from Desulfovibrio vulgaris Hildenborough (DvH) to metal oxides for catalytic CO2 reduction report an in-depth study the resulting enzyme-material interface. Protein film voltammetry (PFV) demonstrates stable binding FDH on metal-oxide electrodes reveals reversible selective formate. Quartz crystal microbalance (QCM) attenuated total...

10.1002/anie.201814419 article EN cc-by Angewandte Chemie International Edition 2019-02-06

Solar-driven coupling of water oxidation with CO2 reduction sustains life on our planet and is high priority in contemporary energy research. Here, we report a photoelectrochemical tandem device that performs photocatalytic to formate. We employ semi-artificial design, which wires W-dependent formate dehydrogenase (FDH) cathode photoanode containing the photosynthetic enzyme, Photosystem II, via synthetic dye complementary light absorption. From biological perspective, system achieves...

10.1021/jacs.8b10247 article EN cc-by Journal of the American Chemical Society 2018-11-19

Reducing CO2 is a challenging chemical transformation that biology solves easily, with high efficiency and specificity. In particular, formate dehydrogenases are of great interest since they reduce to formate, valuable fuel hydrogen storage compound. The metal-dependent prokaryotes can show activity for reduction. Here, we report an expression system produce recombinant W/Sec-FdhAB from Desulfovibrio vulgaris Hildenborough fully loaded cofactors, its catalytic characterization crystal...

10.1021/acscatal.0c00086 article EN ACS Catalysis 2020-02-27

Abstract Storage of solar energy as hydrogen provides a platform towards decarbonizing our economy. One emerging strategy for the production fuels is to use photocatalytic biohybrid systems that combine high catalytic activity non‐photosynthetic microorganisms with light‐harvesting efficiency metal semiconductor nanoparticles. However, few such have been tested H 2 production. We investigated light‐driven by three novel organisms, Desulfovibrio desulfuricans , Citrobacter freundii and...

10.1002/anie.202016960 article EN Angewandte Chemie International Edition 2021-01-16

Lead halide perovskite solar cells are notoriously moisture-sensitive, but recent encapsulation strategies have demonstrated their potential application as photoelectrodes in aqueous solution. However, rely on precious metal co-catalysts, and combination with biological materials remains elusive integrated devices. Here, we interface [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough, a highly active enzyme for H2 generation, triple cation mixed perovskite. The...

10.1021/acsenergylett.9b02437 article EN publisher-specific-oa ACS Energy Letters 2019-12-10

Semiartificial approaches to renewable fuel synthesis exploit the integration of enzymes with synthetic materials for kinetically efficient production. Here, a CO2 reductase, formate dehydrogenase (FDH) from Desulfovibrio vulgaris Hildenborough, is interfaced carbon nanotubes (CNTs) and amorphous dots (a-CDs). Each substrate, tailored electro- photocatalysis, functionalized positive (-NHMe2+) negative (-COO-) chemical surface groups understand optimize electrostatic effect protein...

10.1021/jacs.2c04529 article EN cc-by Journal of the American Chemical Society 2022-07-28

Significance Enzyme bioelectrochemistry concerns the integration of oxidoreductase enzymes into electrodes to enable and study transfer electrons between solid-state material surface biological catalyst. To achieve higher enzyme loading, hence greater current densities, high-surface-area strategies have been employed immobilize enzymes, but these porous electrode architectures amplify formation local chemical gradients. selectivity activity is highly dependent on such changes in environment,...

10.1073/pnas.2114097119 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2022-01-20

Microbial dissimilatory sulfur metabolism utilizing sulfite reductases (Dsr) influenced the biochemical cycle during Earth's history and Dsr pathway is thought to be an ancient metabolic process. Here we performed comparative genomics, phylogenetic, synteny analyses of several proteins involved in or associated with across over 195,000 prokaryotic metagenomes. The results point archaeal origin minimal DsrABCMK(N) protein set, having as primordial function reduction. acquisition additional...

10.1038/s41396-023-01477-y article EN cc-by The ISME Journal 2023-07-19

Abstract Formate production via both CO 2 reduction and cellulose oxidation in a solar‐driven process is achieved by semi‐artificial biohybrid photocatalyst consisting of immobilized formate dehydrogenase on titanium dioxide (TiO | FDH ) producing up to 1.16±0.04 mmol g −1 24 hours at 30 °C 101 kPa under anaerobic conditions. Isotopic labeling experiments with 13 C‐labeled substrates support the mechanism stoichiometric formation through redox half‐reactions. TiO was further hollow glass...

10.1002/anie.202215894 article EN cc-by Angewandte Chemie International Edition 2023-03-08

The electrolysis of dilute CO2 streams suffers from low concentrations dissolved substrate and its rapid depletion at the electrolyte-electrocatalyst interface. These limitations require first energy-intensive capture concentration, before electrolyzers can achieve acceptable performances. For direct electrocatalytic reduction low-concentration sources, we introduce a strategy that mimics carboxysome in cyanobacteria by utilizing microcompartments with nanoconfined enzymes porous electrode....

10.1002/anie.202218782 article EN cc-by Angewandte Chemie International Edition 2023-04-20

Microbial dissimilatory sulfate reduction (DSR) is a key process in the Earth biogeochemical sulfur cycle. In spite of its importance to and carbon cycles, industrial processes, human health, it still not clear how sulfide coupled energy conservation. A central step pathway sulfite by DsrAB reductase, which leads production DsrC-trisulfide. membrane-bound complex, DsrMKJOP, present most organisms that have DsrC, involvement conservation has been inferred from sequence analysis, but precise...

10.1073/pnas.2313650121 article EN Proceedings of the National Academy of Sciences 2024-01-29
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