Inés García‐Rubio

ORCID: 0000-0002-1827-1250
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Research Areas
  • Electron Spin Resonance Studies
  • Photosynthetic Processes and Mechanisms
  • Geomagnetism and Paleomagnetism Studies
  • Crystallization and Solubility Studies
  • X-ray Diffraction in Crystallography
  • Hemoglobin structure and function
  • Geology and Paleoclimatology Research
  • Magnetic and Electromagnetic Effects
  • Skin and Cellular Biology Research
  • Lanthanide and Transition Metal Complexes
  • Metal-Catalyzed Oxygenation Mechanisms
  • Advanced NMR Techniques and Applications
  • Autoimmune Bullous Skin Diseases
  • Cell Adhesion Molecules Research
  • Pharmacogenetics and Drug Metabolism
  • Heme Oxygenase-1 and Carbon Monoxide
  • Electrochemical sensors and biosensors
  • Metalloenzymes and iron-sulfur proteins
  • Metal complexes synthesis and properties
  • Organometallic Complex Synthesis and Catalysis
  • Iron oxide chemistry and applications
  • Geochemistry and Elemental Analysis
  • Porphyrin and Phthalocyanine Chemistry
  • Magnetism in coordination complexes
  • Chemical Analysis and Environmental Impact

ETH Zurich
2009-2025

Universidad de Zaragoza
2000-2025

Hospital Universitario Fundación Jiménez Díaz
2023-2025

Universidad Autónoma de Madrid
2023-2025

Instituto de Investigación de Enfermedades Raras
2025

Centre for Biomedical Network Research on Rare Diseases
2025

Centro de Investigación Biomédica en Red
2025

Instituto de Salud Carlos III
2025

Instituto de Nanociencia y Materiales de Aragón
2008-2024

Centro Universitario de la Defensa
2012-2022

Abstract Intravascular hemolysis can result in hemoglobinuria with acute kidney injury. In this study we systematically explored two vivo animal models and a related cell culture system to identify hemoglobinuria-triggered damage pathways. of stored blood transfusion hemoglobin (Hb) exposure guinea pigs beagle dogs found that led intrarenal conversion ferrous Hb(Fe 2+ ) ferric 3+ ), accumulation free heme Hb-cross-linking products, enhanced 4-hydroxynonenal reactivity renal tissue, tubule...

10.1038/cddis.2015.392 article EN cc-by Cell Death and Disease 2016-01-21

Amyloid aggregation of α-synuclein (αS) is the hallmark Parkinson's disease and other synucleinopathies. Recently, Tau protein, generally associated with Alzheimer's disease, has been linked to αS pathology observed co-localize in αS-rich inclusions, although molecular mechanisms for co-aggregation both proteins remain elusive. We report here that phase-separates into liquid condensates by electrostatic complex coacervation positively charged polypeptides such as Tau. Condensates undergo...

10.1038/s41467-022-32350-9 article EN cc-by Nature Communications 2022-08-06

The first and key step in alkane metabolism is the terminal hydroxylation of alkanes to 1-alkanols, a reaction catalyzed by family integral-membrane diiron enzymes related Pseudomonas putida GPo1 AlkB, diverse group methane, propane, butane monooxygenases some membrane-bound cytochrome P450s. Recently, cytoplasmic P450 was identified prokaryotes that allow their host grow on aliphatic alkanes. One member this family, CYP153A6 from Mycobacterium sp. HXN-1500, hydroxylates medium-chain-length...

10.1128/jb.00286-06 article EN Journal of Bacteriology 2006-06-30

Rationale: Hemolysis occurs not only in conditions such as sickle cell disease and malaria but also during transfusion of stored blood, extracorporeal circulation, sepsis. Cell-free Hb depletes nitric oxide (NO) the vasculature, causing vasoconstriction eventually cardiovascular complications. We hypothesize that Hb-binding proteins may preserve vascular NO signaling hemolysis.Objectives: Characterization an archetypical function by which scavenger could hemolysis.Methods: investigated...

10.1164/rccm.201510-2058oc article EN American Journal of Respiratory and Critical Care Medicine 2015-12-22

Extracellular hemoglobin (Hb) has been recognized as a disease trigger in hemolytic conditions such sickle cell disease, malaria, and blood transfusion. In vivo, many of the adverse effects free Hb can be attenuated by scavenger acute-phase protein haptoglobin (Hp). The primary physiologic disturbances that caused are found within cardiovascular system Hb-triggered oxidative toxicity toward endothelium promoted potential mechanism. molecular mechanisms this well protective activities Hp not...

10.1038/cdd.2013.113 article EN cc-by-nc-sa Cell Death and Differentiation 2013-08-30

The unique monooxygenase activity of cytochrome P450cam has been attributed to coordination a cysteine thiolate the heme cofactor. To investigate this interaction, we replaced with more electron-donating selenocysteine. Good yields selenoenzyme were obtained by bacterial expression an engineered gene containing requisite UGA codon for selenocysteine and simplified yet functional insertion sequence (SECIS). sulfur-to-selenium substitution subtly modulates structural, electronic, catalytic...

10.1073/pnas.0810503106 article EN Proceedings of the National Academy of Sciences 2009-03-18

Abstract Engineering nitrogen fixation in eukaryotes requires high expression of functional nitrogenase structural proteins, a goal that has not yet been achieved. Here we build knowledge-based library containing 32 nifH sequences from prokaryotes diverse ecological niches and metabolic features combine with rapid screening tobacco to identify superior NifH variants for plant mitochondria expression. Three outperform are further tested yeast. Hydrogenobacter thermophilus (Aquificae) is...

10.1038/s42003-020-01536-6 article EN cc-by Communications Biology 2021-01-04

Integrin α6β4 is a major component of hemidesmosomes that mediate the stable anchorage epithelial cells to underlying basement membrane. has also been implicated in cell proliferation and migration carcinoma progression. The third fourth fibronectin type III domains (FnIII-3,4) integrin β4 binding hemidesmosomal proteins BPAG1e BPAG2, participate signalling. Here, it demonstrated X-ray crystallography, small-angle scattering double electron–electron resonance (DEER) complement each other...

10.1107/s1399004715002485 article EN cc-by Acta Crystallographica Section D Biological Crystallography 2015-03-27

Three tris(bipyridine)ruthenium dendrimers bearing either six or eighteen mannose units have been synthesized; encapsulation of the Ru(bipy)3 core alters rate energy and electron transfer as well lectin biosensing abilities.

10.1039/b814146k article EN Chemical Communications 2008-11-26

Bacillus subtilis oxalate decarboxylase (OxDC) catalyzes the conversion of into CO2 and formate. The enzyme is composed two cupin domains, each which contains a Mn(II) ion. Although there general agreement that in N-terminal domain mediates OxDC-catalyzed decarboxylation, legitimate questions have been raised concerning function (if any) bound C-terminal domain. We investigated this problem using series OxDC mutants binding perturbed by mutagenesis Glu-101 Glu-280, coordinate metal...

10.1021/bi801856k article EN Biochemistry 2009-05-27

The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. present study was aimed at examining functionality and elucidating molecular basis for its activation space. Intact rat liver mitochondria neither scavenged nor dismutated externally generated O2*-, unless outer membrane disrupted selectively by digitonin. following disruption largely inhibited bacitracin, an...

10.1042/bj20041683 article EN Biochemical Journal 2005-03-22

Abstract. Flavoproteins are a versatile class of proteins involved in numerous biological processes, including redox reactions, electron transfer, and signal transduction, often relying on their ability to stabilize different oxidation states flavin cofactor. A critical feature cofactors is capacity achieve, within particular protein environments, semiquinone state that plays pivotal role mediating single-electron transfer events key understanding flavoprotein reactivity. Hyperfine...

10.5194/mr-2024-24 preprint EN cc-by 2025-01-17

A HYSCORE investigation of the heme center in cytochrome b(559) is presented. To assign observed signals to specific nuclei, bis-imidazol coordinated compounds that model iron environment are also studied. In selective isotopic substitution nitrogen atoms has been performed. The spectra allow us obtain hyperfine and quadrupolar coupling tensors imidazol bonding atoms. results can be interpreted terms structure electronic distribution active center. indicate unpaired electron confined a...

10.1021/ja035364g article EN Journal of the American Chemical Society 2003-11-22
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