Related Experiment Video
Updated: Nov 2, 2025
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Calcium-Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores
Natasha P Vargo1, Jill B Harland2, Bradley W Musselman2
1Department of Chemistry, Brown University, 324 Brook Street, Providence, RI, 02912, USA.
Abstract:
Coupled dinuclear copper oxygen cores (Cu2 O2 ) featured in type III copper proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for O2 transport and substrate oxidation in many organisms. μ-1,2-cis peroxido dicopper cores (C P) have been proposed as key structures in the early stages of O2 binding in these proteins; their reversible isomerization to other Cu2 O2 cores are directly relevant to enzyme function. Despite the relevance of such species to type III copper proteins and the broader interest in the properties and reactivity of bimetallic C P cores in biological and synthetic systems, the properties and reactivity of C P Cu2 O2 species remain largely unexplored. Herein, we report the reversible interconversion of μ-1,2-trans peroxido (T P) and C P dicopper cores. CaII mediates this process by reversible binding at the Cu2 O2 core, highlighting the unique capability for metal-ion binding events to stabilize novel reactive fragments and control O2 activation in biomimetic systems.
More Related Videos
11:04Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
Published on: September 7, 2019
14:34Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay
Published on: December 25, 2021
Related Concept Videos
03:02Colors and Magnetism
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
01:16Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
01:17Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
01:19Complexation Equilibria: The Chelate Effect
02:51Metal-Ligand Bonds
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
02:58Crystal Field Theory - Octahedral Complexes
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...