A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
Authors
Keywords
-
Journal
Chemical Science
Volume 9, Issue 7, Pages 1989-1995
Publisher
Royal Society of Chemistry (RSC)
Online
2018-01-15
DOI
10.1039/c7sc04732k
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- A question of flexibility in cytochrome c oxidase models
- (2017) Pauline Vorburger et al. INORGANICA CHIMICA ACTA
- Phenol-Induced O–O Bond Cleavage in a Low-Spin Heme–Peroxo–Copper Complex: Implications for O2 Reduction in Heme–Copper Oxidases
- (2017) Andrew W. Schaefer et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- From Models of Hemoproteins to Self-Assembled Molecular Wires
- (2017) Christophe Kahlfuss et al. ChemPlusChem
- Intramolecular OxidativeO-Demethylation of an Oxoferryl Porphyrin Complexed with a Per-O-methylated β-Cyclodextrin Dimer
- (2016) Hiroaki Kitagishi et al. Chemistry-An Asian Journal
- Critical Aspects of Heme–Peroxo–Cu Complex Structure and Nature of Proton Source Dictate Metal–Operoxo Breakage versus Reductive O–O Cleavage Chemistry
- (2016) Suzanne M. Adam et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases
- (2016) Ambika Bhagi-Damodaran et al. Nature Chemistry
- Synthetic Heme/Copper Assemblies: Toward an Understanding of Cytochrome c Oxidase Interactions with Dioxygen and Nitrogen Oxides
- (2015) Shabnam Hematian et al. ACCOUNTS OF CHEMICAL RESEARCH
- Reaction Mechanism of Cytochrome c Oxidase
- (2015) Shinya Yoshikawa et al. CHEMICAL REVIEWS
- Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction
- (2015) Sudipta Chatterjee et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Supramolecular Iron Porphyrin/Cyclodextrin Dimer Complex that Mimics the Functions of Hemoglobin and Methemoglobin
- (2013) Kenji Watanabe et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Effect of coordinated ligands on antiproliferative activity and DNA cleavage property of three mononuclear Cu(II)-terpyridine complexes
- (2012) Verasuntharam M. Manikandamathavan et al. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
- Comparative studies in series of cytochrome c oxidase models
- (2011) F. Melin et al. JOURNAL OF INORGANIC BIOCHEMISTRY
- Homogeneous catalytic O2 reduction to water by a cytochrome c oxidase model with trapping of intermediates and mechanistic insights
- (2011) Z. Halime et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Oxoferryl Porphyrin/Hydrogen Peroxide System Whose Behavior is Equivalent to Hydroperoxoferric Porphyrin
- (2010) Hiroaki Kitagishi et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Bovine cytochromecoxidase structures enable O2reduction with minimization of reactive oxygens and provide a proton-pumping gate
- (2010) Kazumasa Muramoto et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Combined Microspectrophotometric and Crystallographic Examination of Chemically Reduced and X-ray Radiation-Reduced Forms of Cytochromeba3Oxidase fromThermus thermophilus: Structure of the Reduced Form of the Enzyme†
- (2009) Bin Liu et al. BIOCHEMISTRY
- Catalytic Reduction of O2by CytochromecUsing a Synthetic Model of CytochromecOxidase
- (2009) James P. Collman et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started