about
Isolation and characterization of the gene coding for human cytidine deaminaseSynthesis of the H-cluster framework of iron-only hydrogenase.Computational approaches to shed light on molecular mechanisms in biological processesNitrosyl derivatives of diiron(I) dithiolates mimic the structure and Lewis acidity of the [FeFe]-hydrogenase active site.Redox non-innocence of a N-heterocyclic nitrenium cation bound to a nickel-cyclam core.Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126.Impact of Cadmium on Intracellular Zinc Levels in HepG2 Cells: Quantitative Evaluations and Molecular Effects.Does the environment around the H-cluster allow coordination of the pendant amine to the catalytic iron center in [FeFe] hydrogenases? Answers from theory.Dissecting the intimate mechanism of cyanation of {2Fe3S} complexes related to the active site of all-iron hydrogenases by DFT analysis of energetics, transition states, intermediates and products in the carbonyl substitution pathway.Asymmetric biomimetic oxidations of phenols: the mechanism of the diastereo- and enantioselective synthesis of thomasidioic acid.A new FeMo complex as a model of heterobimetallic assemblies in natural systems: Mössbauer and density functional theory investigations.Targeting intermediates of [FeFe]-hydrogenase by CO and CN vibrational signatures.Tailoring transition metal complexes for nonlinear optics applications. 2. A theoretical investigation of the second-order nonlinear optical properties of M(CO)(5)L complexes (M = Cr, W; L = Py, PyCHO, Pyz, PyzBF(3), BPE, BPEBF(3)).Disclosure of key stereoelectronic factors for efficient H2 binding and cleavage in the active site of [NiFe]-hydrogenases.Functionally relevant interplay between the Fe(4)S(4) cluster and CN(-) ligands in the active site of [FeFe]-hydrogenases.Asymmetric biomimetic oxidations of phenols using oxazolidines as chiral auxiliaries: the enantioselective synthesis of (+)- and (−)-dehydrodiconiferyl alcoholThe regiochemistry of the NO3-promoted gas phase nitration of toluene and phenol with NO2A theoretical study of spin states in Ni-S4 complexes and models of the [NiFe] hydrogenase active siteThe oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-clusterCombining experimental and theoretical methods to learn about the reactivity of gas-processing metalloenzymesInfluence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspectivetrans versus geminal electron delocalization in tetra- and diethynylethenes: a new method of analysisDFT investigation of structural, electronic, and catalytic properties of diiron complexes related to the [2Fe](H) subcluster of Fe-only hydrogenasesInsights into the mechanism of electrocatalytic hydrogen evolution mediated by Fe2(S2C3H6)(CO)6: the simplest functional model of the Fe-hydrogenase active siteA QM/MM investigation of the activation and catalytic mechanism of Fe-only hydrogenasesStructural insights into the active-ready form of [FeFe]-hydrogenase and mechanistic details of its inhibition by carbon monoxideElectron delocalization in linearly pi-conjugated systems: a concept for quantitative analysisDFT Investigation of H2 activation by [M(NHPnPr3)('S3')] (M = Ni, Pd). Insight into key factors relevant to the design of hydrogenase functional modelsStructural and electronic properties of the [FeFe] hydrogenase H-cluster in different redox and protonation states. A DFT investigationStructure and energetics of Fe2(CO)8 singlet and triplet electronic statesThrough versus cross electron delocalization in polytriacetylene oligomers: a computational analysisProbing the effects of one-electron reduction and protonation on the electronic properties of the Fe-S clusters in the active-ready form of [FeFe]-hydrogenases. A QM/MM investigationIsocyanide in biochemistry? A theoretical investigation of the electronic effects and energetics of cyanide ligand protonation in [FeFe]-hydrogenasesStructural variations, electrochemical properties and computational studies on monomeric and dimeric Fe-Cu carbide clusters, forming copper-based staple arraysSpeciation of copper-peptide complexes in water solution using DFTB and DFT approaches: case of the [Cu(HGGG)(Py)] complexElectrocatalytic dihydrogen evolution mechanism of [Fe2(CO)4(kappa(2)-Ph2PCH2CH2PPh2)(mu-S(CH2)3S)] and related models of the [FeFe]-hydrogenases active site: a DFT investigationInvestigations on the role of proton-coupled electron transfer in hydrogen activation by [FeFe]-hydrogenaseA Scheme for the Evaluation of Electron Delocalization and Conjugation Efficiency in Linearly π-Conjugated SystemsQuantum mechanical methods for the investigation of metalloproteins and related bioinorganic compoundsFeMo Heterobimetallic Dithiolate Complexes: Investigation of Their Electron Transfer Chemistry and Reactivity toward Acids, a Density Functional Theory Rationalization
P50
Q28293052-49F9AEDD-DF4A-4451-9733-E8742909102CQ34392892-5B0BD4FC-F609-477C-ADC6-5FED641D0939Q34671563-58C58FDE-E5C3-43EA-AE89-DD906D05E840Q36952611-82273183-DDD9-480F-A49A-59C1F40B2B63Q37603916-72E3CE6C-607F-4942-8554-E9556E1DFAB4Q41954090-FCBAEAB6-A27B-4CCC-AB89-5B2AB5DB4A08Q41995140-4BE7B2B9-AC92-4C21-8F98-4CD1BCD829C9Q44304466-BC61C422-C4AF-4257-9695-36DA9383D90AQ45172665-1805635B-CF92-4626-86C6-91BE154D092AQ46765208-BEA6287B-E3C2-48C2-83FC-F4128FFED65FQ46823516-F5040073-FB20-4B7F-8C82-72141DA06AFCQ50541574-92857DD2-EBB5-422E-85C4-7DDD3F887C94Q51156316-B2E27A14-922F-4F31-B8F8-86930E241472Q53074595-3649B582-39DA-4011-979A-1AF758E5E034Q53970202-677F608A-AA68-4BD9-AB39-FC806126B112Q57715973-5EE52281-B1F7-4738-983A-A40611BCDDBCQ57715980-2DBDA699-F4A8-4DF9-84AF-4D371019C3C0Q57905489-3EE5945E-56D7-4FFD-A60E-78B43816338CQ60211921-1CF8AD48-91E0-4232-B2DA-163D0ABF1A9FQ60211923-9C8386F4-6415-4EF4-810B-168E59763EB2Q62112717-7C57A0E9-B355-4FD2-AB5A-EB9E825D2CDBQ77150769-0BA8ADEF-1981-4F5E-968E-8B003506B8B3Q77769758-28E06AF7-0C94-4D0B-90C1-F9D0319AF6C3Q79469010-5303E8E4-CBF2-41F4-8F02-308CB79D5DA4Q80549119-B41FB15E-36E4-4B89-9098-03DBFB596675Q80739682-0A5F135D-E40E-4BC1-AC6F-33ECB731590CQ80834405-2B112123-10BE-43ED-A0B4-0837D5573052Q81239193-FCF84255-7732-42F0-B758-BD002F9776C7Q81424395-2BAC0A32-F167-4291-87B6-AC90E82D593BQ81564532-ADB08AB7-A365-4A2F-A9B7-244C25B55484Q81594240-1D4DA527-E0CA-4FA7-BF5E-A3E8FF1FBCC3Q82507446-3FC20347-111B-4B77-830F-FE443DDEF19EQ83316726-4B80E339-63C9-4C3D-AC9C-2F0D5562CD8AQ83773508-F0CDF5D2-E73D-406A-A329-2650EF51F4E8Q84002937-1B746333-9B2F-4B97-964F-DD1C6DADDEF2Q84510560-060B778D-F31E-438A-91A0-1718BA64516AQ85688779-6C71D622-B9BC-48C9-983F-CBF035D504A5Q86813776-43E0EC47-D245-4A9E-BBB7-07953A3CDC79Q87462417-8E86486A-C7A5-4BD3-9C25-8CE3BE52FD37Q90607930-75E45BC2-3B5C-4921-AEC6-160FFA597192
P50
description
researcher, ORCID id # 0000-0002-5709-818X
@en
wetenschapper
@nl
name
Maurizio Bruschi
@ast
Maurizio Bruschi
@en
Maurizio Bruschi
@es
Maurizio Bruschi
@nl
type
label
Maurizio Bruschi
@ast
Maurizio Bruschi
@en
Maurizio Bruschi
@es
Maurizio Bruschi
@nl
prefLabel
Maurizio Bruschi
@ast
Maurizio Bruschi
@en
Maurizio Bruschi
@es
Maurizio Bruschi
@nl
P106
P1153
36058478300
P31
P496
0000-0002-5709-818X