Mono-nuclear copper complexes mimicking the intermediates for the binuclear copper center of the subunit II of cytochrome oxidase: a peptide based approach
Author:
Affiliation:
1. Tata Institute of Fundamental Research
2. Mumbai 400 005
3. India
4. Department of Lipid Science
5. Central Food Technological Research Institute
6. Mysore-570020
Abstract
Novel copper peptides derived from the subunit-II of cytochrome oxidase mimic the intermediates in the pathway of the purple CuA center.
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/DT/C6DT02977A
Reference34 articles.
1. Metal-binding sites in proteins
2. Mechanism of Copper Incorporation in Subunit II of Cytochrome c Oxidase from Thermus thermophilus: Identification of Intermediate Species
3. Kinetics of Copper Incorporation into a Biosynthetic Purple CuA Azurin: Characterization of Red, Blue, and a New Intermediate Species
4. Reaction Mechanism of Cytochrome c Oxidase
5. The CuA Center of a Soluble Domain from Thermus Cytochrome ba3. An NMR Investigation of the Paramagnetic Protein
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1. Synthesis and photophysical properties of dinuclear N-heterocyclic carbene (NHC) copper(I) complexes and their application to photoluminescent light-emitting diodes and anti-counterfeiting;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2024-03
2. Identification of a copper ion recognition peptide sequence in the subunit II of cytochrome c oxidase: a combined theoretical and experimental study;JBIC Journal of Biological Inorganic Chemistry;2021-04-29
3. Structural Basis for a Quadratic Relationship between Electronic Absorption and Electronic Paramagnetic Resonance Parameters of Type 1 Copper Proteins;Inorganic Chemistry;2020-07-20
4. A Binuclear CuA Center Designed in an All α-Helical Protein Scaffold;Journal of the American Chemical Society;2020-07-14
5. A comparative study on the nickel binding ability of peptides containing separate cysteinyl residues;Dalton Transactions;2019
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