about
The crystal structure of halofantrine-ferriprotoporphyrin IX and the mechanism of action of arylmethanol antimalarialsSpeciation and structure of ferriprotoporphyrin IX in aqueous solution: spectroscopic and diffusion measurements demonstrate dimerization, but not mu-oxo dimer formation.Molecular modeling of the mechanochemical triggering mechanism for catalysis of carbon-cobalt bond homolysis in coenzyme B12.Synthesis of copper and zinc 2-(pyridin-2-yl)imidazo[1,2-a]pyridine complexes and their potential anticancer activity.Analysis of malaria pigment from Plasmodium falciparum.Bis-(2-hy-droxy-eth-yl)ammonium 2-bromo-phenolate.Insights into porphyrin chemistry provided by the microperoxidases, the haempeptides derived from cytochrome c.NMR spectroscopy and molecular modelling studies of nitrosylcobalamin: further evidence that the deprotonated, base-off form is important for nitrosylcobalamin in solution.Structure-function relationships in aminoquinolines: effect of amino and chloro groups on quinoline-hematin complex formation, inhibition of beta-hematin formation, and antiplasmodial activity.Thermodynamic factors controlling the interaction of quinoline antimalarial drugs with ferriprotoporphyrin IX.The interaction of the heme-octapeptide, N-acetylmicroperoxidase-8 with antimalarial drugs: solution studies and modeling by molecular mechanics methods.Fate of haem iron in the malaria parasite Plasmodium falciparum.N,N'-bis(2-hydroxycyclohexyl)-N,N'-bis(2-hydroxyethyl)ethane-1,2-diaminium dichloride.Amino-alcohol ligands: synthesis and structure of N,N'-bis(2-hydroxycyclopentyl)ethane-1,2-diamine and its salts, and an assessment of its fitness and that of related ligands for complexing metal ions.Hydrogen-bonding controls the solid-state and enantiomeric conformations of the amino alcohol ligand 2-[(2-hydroxyethyl)amino]cyclohexanol.Phenylvinylcobalamin: an alkenylcobalamin featuring a ligand with a large trans influence.Solution structure, enzymatic, and non-enzymatic reactivity of 3-isoadenosylcobalamin, a structural isomer of coenzyme B12 with surprising coenzymic activity.Diisopropylphosphitocobalamin-acetone-water (1/3.48/7.56).Isoamylcobalamin-acetone-water (1/0.385/12.650).DFT-UX3LYP studies on the coordination chemistry of Ni2+. Part 1: Six coordinate [Ni(NH3)n(H2O)(6-n)]2+ complexes.Probing the nature of the Co(III) ion in cobalamins: a comparison of the reaction of aquacobalamin (vitamin B12a) and aqua-10-chlorocobalamin with some anionic and N-donor ligands.Outer-sphere anion recognition by a cyclen-based octadentate europium(III) complex: pH dependent recognition of ortho-phthalic acid.cis influence in models of cobalt corrins by DFT and TD-DFT studies.Influence of electronic and steric effects on stability constants and electrochemical reversibility of divalent ion complexes with glycine and sarcosine. A glass electrode potentiometric, sampled direct current polarographic, virtual potentiometric,The synthesis of a corrole analogue of aquacobalamin (vitamin B12a) and its ligand substitution reactions.The preparation of N-acetyl-Co(III)-microperoxidase-8 (NAcCoMP8) and its ligand substitution reactions: a comparison with aquacobalamin (vitamin B(12a)).Hemepeptide models for hemoproteins: the behavior of N-acetylmicroperoxidase-11 in aqueous solution.Kinetics of the release of aluminum from human serum dialuminum transferrin to citrate.Revealing Factors Influencing the Fluorine-Centered Non-Covalent Interactions in Some Fluorine-Substituted Molecular Complexes: Insights from First-Principles Studies.A Density Functional Theory and Quantum Theory of Atoms-in-Molecules Analysis of the Stability of Ni(II) Complexes of Some Amino Alcohol LigandsSignificance of hydrogen bonding and other noncovalent interactions in determining octahedral tilting in the CHNHPbI hybrid organic-inorganic halide perovskite solar cell semiconductorIs the Fluorine in Molecules Dispersive? Is Molecular Electrostatic Potential a Valid Property to Explore Fluorine-Centered Non-Covalent Interactions?The effects of anions on the kinetics of reductive elimination of iron from monoferrictransferrins by thiolsHemes and hemoproteins. 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solutionHemes and hemeproteins, 2: The pH-dependent equilibria of microperoxidase-8 and characterization of the coordination sphere of Fe(III)Hemes and hemoproteins. 3. The reaction of microperoxidase-8 with cyanide: comparison with aquocobalamin and hemoproteinsProtein-free models for the proton-coupled reduction of haemoproteinsRelease of iron from C-terminal monoferric transferrin to phosphate and pyrophosphate at pH 5.5 proceeds through two pathwaysStructural and enzymatic studies of a new analogue of coenzyme B12 with an alpha-adenosyl upper axial ligandThe physical chemistry of coordinated aqua-, ammine-, and mixed-ligand Co2+ complexes: DFT studies on the structure, energetics, and topological properties of the electron density
P50
Q28281690-31A2AAC6-3DB6-4E0D-96B0-E21D7CCDFC7BQ31061011-47602FFD-D78E-4CE4-B8C1-48039B87D69CQ32120659-7A86C966-2175-46A5-91A9-48BC318B7398Q32184433-87711278-41A6-492D-A9C0-5C9FAECEB719Q34316957-E86D3D77-753A-4B15-B2EA-F5462F52C5DCQ36214113-8F1D1416-D53E-486A-B9DA-1A5A8701C54FQ36957506-F1791D5F-A858-47D5-B5EF-2DFAC1627F2CQ37369403-3E6977A3-193A-4E79-86E7-9F62E879256FQ41922383-BD96E2B7-19AA-426F-B319-0EB6298813DAQ41927677-A63B1197-184A-4380-8870-DF8277E789FEQ41930101-DB0EE8E3-AB7D-4BBB-AF44-793F6317D325Q42145596-CEF7D4EC-5BE7-4632-ADC9-0F2A1D29F857Q42836229-DFD41825-E4C4-4879-8FDA-4E1080CB4CFCQ42946981-FE11E4FF-93EA-4A25-8AFB-0FF91F427302Q43114355-E970ACBF-EF30-4538-B579-DFCC2F4C69EBQ43866823-2C6C764C-C012-4238-AD39-4673CD47C07DQ44732488-FF8A5C58-0934-4C11-B176-2F117505312FQ44758621-8BD53B4E-5DFB-4734-AC40-1E30BD006ED8Q44835212-267E3B8F-A63B-4C2D-A857-C2ED1036714DQ45098903-701BED54-52EC-48AA-A6B4-430C2BE41ACBQ45278949-432E2CAC-3FA2-436D-AC90-6972501A8632Q46148326-0B441104-079E-4AD8-83F2-8932D90CC82FQ46211002-AF751E9F-6D6E-40BE-A75D-25057246B529Q46260690-866FAB17-DA98-41DE-9296-D42A728DC886Q46685508-9A041B01-049D-441C-8DCC-491416D85CFFQ46827188-BE919BDE-D99C-4A2A-8DB4-1E3043FCC25DQ46960364-1E22A98C-7F33-4081-B782-ECDDC6D103F8Q46987360-9495D398-D604-49CB-A6AC-2F46FC2F82B7Q52640845-F6CBFC8C-CC4D-49D0-8C78-2625D95807FFQ56999162-D069D543-BDFC-4541-AC1E-1D0EE913A157Q60912895-BF9B76C4-B87E-462B-B3FA-B28B5540FE09Q64267960-69F66BE5-B224-4786-8CF8-623D3CF33B7AQ68736565-34105DE7-A1F4-4D83-89B8-A7FAA6A51A43Q70146414-984313FC-4FDA-4726-B535-9733F86B86F1Q70146415-7F13083E-914E-4A1B-84B7-B46F9038BE3BQ70171175-E1444851-8C54-442A-A967-9C76322043D2Q70190911-EF66D805-4175-41BC-8F00-08F6905B876FQ72593675-978CF9BF-3A15-4610-BC65-1001AC709C74Q74765339-93F4C1A5-E14B-4BE7-BF21-69F1F2C532FEQ82947876-790813F8-B90B-4975-8B35-7AA703098DF0
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Helder M Marques
@ast
Helder M Marques
@es
Helder M Marques
@nl
Helder M Marques
@sl
Helder M. Marques
@en
type
label
Helder M Marques
@ast
Helder M Marques
@es
Helder M Marques
@nl
Helder M Marques
@sl
Helder M. Marques
@en
altLabel
Helder M Marques
@en
Helder Marques
@en
prefLabel
Helder M Marques
@ast
Helder M Marques
@es
Helder M Marques
@nl
Helder M Marques
@sl
Helder M. Marques
@en
P106
P31
P496
0000-0003-1675-3835