about
A novel type of catalytic copper cluster in nitrous oxide reductaseKinetic, structural, and EPR studies reveal that aldehyde oxidoreductase from Desulfovibrio gigas does not need a sulfido ligand for catalysis and give evidence for a direct Mo-C interaction in a biological systemBiochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774The first crystal structure of class III superoxide reductase from Treponema pallidum.Improving sample treatment for in-solution protein identification by peptide mass fingerprint using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Simplifying sample handling for protein identification by peptide mass fingerprint using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Influence of the protein staining in the fast ultrasonic sample treatment for protein identification through peptide mass fingerprint and matrix-assisted laser desorption ionization time of flight mass spectrometry.Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductaseCan ultrasonic energy efficiently speed (18)O-labeling of proteins?Analysis of resonance Raman data on the blue copper site in pseudoazurin: excited state π and σ charge transfer distortions and their relation to ground state reorganization energy.Low-spin heme b(3) in the catalytic center of nitric oxide reductase from Pseudomonas nautica.The anaerobe-specific orange protein complex of Desulfovibrio vulgaris hildenborough is encoded by two divergent operons coregulated by σ54 and a cognate transcriptional regulator.SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes.Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase: redox dependence and insight into reactivityDetermination of the active form of the tetranuclear copper sulfur cluster in nitrous oxide reductase.The small iron-sulfur protein from the ORP operon binds a [2Fe-2S] cluster.Superoxide reductase from the syphilis spirochete Treponema pallidum: crystallization and structure determination using soft X-rays.Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis.DNA damage and metal accumulation in four tissues of feral Octopus vulgaris from two coastal areas in Portugal.Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617.Crystallization and preliminary X-ray diffraction analysis of two pH-dependent forms of a di-haem cytochrome c peroxidase from Pseudomonas nautica.Spectroscopic and electronic structure studies of the mu(4)-sulfide bridged tetranuclear Cu(Z) cluster in N(2)O reductase: molecular insight into the catalytic mechanism.Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri.Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri.Isolation and characterization of a new Cu-Fe protein from Desulfovibrio aminophilus DSM12254.Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans containing more than one cytochrome.Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase.Crystallization and preliminary X-ray diffraction analysis of the 16-haem cytochrome of Desulfovibrio gigas.Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase.Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study.Gas chromatography mass spectrometry determination of acaricides from honey after a new fast ultrasonic-based solid phase micro-extraction sample treatment.Electron transfer complex between nitrous oxide reductase and cytochrome c552 from Pseudomonas nautica: kinetic, nuclear magnetic resonance, and docking studies.The catalytic cycle of nitrous oxide reductase - The enzyme that catalyzes the last step of denitrification.Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135.Superoxide reductase: different interaction modes with its two redox partners.Spectroscopic Definition of the CuZ° Intermediate in Turnover of Nitrous Oxide Reductase and Molecular Insight into the Catalytic Mechanism.A new type of metal-binding site in cobalt- and zinc-containing adenylate kinases isolated from sulfate-reducers Desulfovibrio gigas and Desulfovibrio desulfuricans ATCC 27774.Copper-containing nitrite reductase from Pseudomonas chlororaphis DSM 50135.A variable temperature spectroscopic study on Paracoccuspantotrophus pseudoazurin: protein constraints on the blue Cu site.Insights into the Molybdenum/Copper Heterometallic Cluster Assembly in the Orange Protein: Probing Intermolecular Interactions with an Artificial Metal-Binding ATCUN Tag.
P50
Q27621620-66B455C7-1760-4D90-9DFC-2F98708BA0C0Q27655558-5EBFFF8B-5E53-463F-B07B-A8AF45058BC4Q28144923-9951D515-51EC-4556-8CD7-556A06B81E07Q30159757-5A65A080-8461-4216-B3E0-5A1CFA625441Q33293367-5205FD62-B034-4CF0-BF47-7BB7B28C164DQ33299531-C132455F-B2D3-4A8C-8A74-29A0AA048345Q33328085-4582E374-76EC-48FB-844A-1C1897FAF0AFQ33412211-A19BD969-66BB-4C66-B527-2896FAB9BC17Q33509058-E6496DB4-169C-4B5F-8EB5-E4D10933E232Q34258727-EDF4DCF6-E50A-4F09-8C1F-7BCA9864B120Q34988112-9D877328-D888-435C-ACAA-DE9F7D3B401AQ35096330-C3D0268D-4A24-403E-872C-820350918B4DQ35668764-8E2DA5E9-A8D3-4D66-A062-336C9A378844Q36093551-7C5905D7-9933-48E4-B0AE-6CF17AEC6082Q37590349-B1C0AF25-735E-448D-83CA-AAC87F06CD74Q39725454-E9F5ED5B-1CFC-48D4-819B-046065EFE5B0Q42120285-A91778A3-0A4F-47BE-A166-3B533708CD90Q42231165-3236A271-C8D4-41D4-BD5C-AA006780A1ADQ42475904-073B82E3-9B26-450D-84A0-EA5861F5435FQ42632180-5AA18089-9A64-4906-BBB7-401D32F35C76Q43933265-1DA0F302-E531-46A0-BDB1-4CD87331D101Q44115874-90A1947A-F638-4D9D-925D-8736D1DE81C7Q44234889-AD639F79-3220-4346-B8AF-9E1B7949902DQ44294863-3667D13B-4E39-445E-B460-948AE30D6C23Q44407809-C3656A93-8EF1-4D79-91FE-32C386E92D46Q44615795-1F81804E-75BA-4FC7-AA0E-2C2678156B5CQ44805038-E34A0487-47D4-447F-BDEE-A3320A6A8E62Q44855123-0BDB7AC6-6841-4E46-979A-32C7CA31B7B8Q45058621-3C3C775C-68C6-4777-84BC-D978F7372DBCQ45246756-DF4A78D8-2996-4726-9F99-68E1520AA8CCQ46204865-95674088-17BB-4D9E-A197-CD55E05A0AA4Q46247500-EE32D616-27DB-4E03-AF9E-253B681678C8Q46304321-9E17242D-F031-40A2-9017-56A44722C8CBQ46416908-18B516BC-AD18-40B9-B1D2-7395D1BB0276Q46550919-59EA3DA9-E5CC-4241-B5C9-6C5E2A582F77Q46571318-F8C52E25-D58C-43DD-AEF2-DCF90BE8A95DQ46712198-61B836F9-E1DB-4F4E-ACCD-84AECE4EEE92Q47383603-D308ADD8-7034-4FD4-9025-8C597D4378F1Q47690887-57D09BD0-04F5-44D0-B4BA-92B4C970BF6DQ48030129-960591CA-C7EC-42B4-BC49-819AED0696A4
P50
description
hulumtuese
@sq
researcher
@en
ricercatrice
@it
wetenschapper
@nl
հետազոտող
@hy
name
Isabel Moura
@ast
Isabel Moura
@en
Isabel Moura
@es
Isabel Moura
@nl
Isabel Moura
@sl
type
label
Isabel Moura
@ast
Isabel Moura
@en
Isabel Moura
@es
Isabel Moura
@nl
Isabel Moura
@sl
altLabel
Isabel Moura
@en
prefLabel
Isabel Moura
@ast
Isabel Moura
@en
Isabel Moura
@es
Isabel Moura
@nl
Isabel Moura
@sl
P214
P1053
D-6339-2013
P106
P1153
55937240200
7102887093
P21
P213
0000 0000 6830 9339
P214
P31
P3829
P496
0000-0003-0971-4977