about
Structural, EPR superhyperfine, and NMR hyperfine properties of the Cu-octarepeat binding site in the prion protein.Solid-state ¹⁷O NMR spectroscopy of paramagnetic coordination compounds.Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand.Hydride Attack on a Coordinated Ferric Nitrosyl: Experimental and DFT Evidence for the Formation of a Heme Model-HNO DerivativeHNO-Binding in Heme Proteins: Effects of Iron Oxidation State, Axial Ligand, and Protein Environment.Inhibition of Aβ42 peptide aggregation by a binuclear ruthenium(II)-platinum(II) complex: Potential for multi-metal organometallics as anti-amyloid agents.Iron porphyrin carbenes as catalytic intermediates: structures, Mössbauer and NMR spectroscopic properties, and bondingIsoprenoid biosynthesis: ferraoxetane or allyl anion mechanism for IspH catalysis?Over or under: hydride attack at the metal versus the coordinated nitrosyl ligand in ferric nitrosyl porphyrins.C-H Insertions by Iron Porphyrin Carbene: Basic Mechanism and Origin of Substrate Selectivity.Lewis Acid Activation of the Ferrous Heme-NO Fragment toward the N-N Coupling Reaction with NO To Generate N2O.A distonic radical-ion for detection of traces of adventitious molecular oxygen (O2) in collision gases used in tandem mass spectrometers.Bisphosphonate-Generated ATP-Analogs Inhibit Cell Signaling Pathways.Catalytic Role of Conserved Asparagine, Glutamine, Serine, and Tyrosine Residues in Isoprenoid Biosynthesis EnzymesNot Limited to Iron: A Cobalt Heme-NO Model Facilitates N-N Coupling with External NO in the Presence of a Lewis Acid to Generate N2 OBiocatalytic Strategy for Highly Diastereo- and Enantioselective Synthesis of 2,3-Dihydrobenzofuran-Based Tricyclic ScaffoldsMechanistic Investigation of Biocatalytic Heme Carbenoid Si-H Insertions
P50
Q33830831-1289C106-21A6-49C6-B126-47E0F4C23CEDQ35566120-931BA45F-E0FA-421E-8F33-EEE7DB4A24BBQ35787250-2D10A648-3662-4DF9-9923-1EB025A0CA3AQ36531461-5C76B0A6-DAE8-49E1-88E5-0281D46C96B8Q39232703-ADF3A074-E463-4AF3-932A-7DA43312C2D3Q41679481-F1C1D99E-053A-4539-98FF-F63A84FCF8AEQ42773713-19BF9DA1-1E90-4507-91E9-22E8468BBDBBQ42917508-758C3F61-69E9-4F36-AC9F-CADB5854E7A9Q47135993-4B24266A-7F0B-4409-9669-4A5DE464C589Q47601887-01801AE7-6CA8-4070-9BD9-12088AFD6C65Q52675377-D114D623-1FC2-4544-A818-CC5EE165A61FQ53508065-E3007358-FA3A-465E-9107-5A43C6FBDA70Q54978574-8B15D4A7-3046-49D7-A923-E19928E4000BQ57825623-F5AFA973-D50F-4D0C-AD00-7CE810EC19AAQ90578524-F0B41A78-DBB1-49E5-906A-580EF76266C0Q92111986-B47FB0EB-D6BF-4104-9BEA-2805F3FD693BQ92713299-A6DD5032-D337-49A7-8644-4241274D91FB
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Rahul L Khade
@en
Rahul L Khade
@nl
type
label
Rahul L Khade
@en
Rahul L Khade
@nl
prefLabel
Rahul L Khade
@en
Rahul L Khade
@nl
P31
P496
0000-0003-3212-7949