Superoxo, μ-peroxo, and μ-oxo complexes from heme/O
 2
 and heme-Cu/O
 2
 reactivity: Copper ligand influences in cytochrome
 c
 oxidase models

Kim, Eunsuk; Helton, Matthew E.; Wasser, Ian M.; Karlin, Kenneth D.; Shen, Lu; Huang, Hongwei; Moënne‐Loccoz, Pierre; Incarvito, Christopher D.; Rheingold, Arnold L.; Honecker, Marcus; Kaderli, Susan; Zuberbühler, Andreas D.

doi:10.1073/pnas.0737180100

Cited by 99 publications

(118 citation statements)

References 46 publications

(18 reference statements)

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“…Titrations indicating 1:1 uptake of O 2 for each [(F 8 )Fe II ] precursor also strongly supports the [(THF)(F 8 )Fe III (O 2 •− )] formulation. Confirmation that this complex is best described as an iron(III)-superoxide species, in terms of its electronic structure, come from resonance Raman spectroscopy: ν (O–O) = 1178 cm −1 [Δ( 18 O 2 ) −64 cm −1 ], ν (Fe–O) = 569 cm −1 [Δ( 18 O 2 ) −24 cm −1 ] [44, 45]. …”

Section: Resultsmentioning

confidence: 99%

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

Sharma

Karlin

2013

Polyhedron

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Inspired by the chemistry relevant to dioxygen storage, transport and activation by metalloproteins, in particular for heme/copper oxidases, and carbon monoxide binding to metal-containing active sites as a probe or surrogate for dioxygen binding, a series of heme derived dioxygen and CO complexes have been designed, synthesized, and characterized with respect to their physical properties and reactivity. The focus of this study is in the description and comparison of three types heme-superoxo and heme-CO adducts. The starting point is in the characterization of the reduced heme complexes, [(F8)FeII], [(PPy)FeII] and [(PIm)FeII], where F8, PPy and PIm are iron(II)-porphyrinates and where PPy and PIm possess a covalently tethered axial base pyridyl or imidazolyl group, respectively. The spin-state properties of these complexes vary with solvent. The low temperature reaction between O2 and these reduced porphyrin FeII complex yield distinctive low spin heme-superoxo adducts. The dioxygen binding properties for all three complexes are shown to be reversible, via alternate argon or O2 bubbling. Carbon monoxide binds to the reduced heme-FeII precursors to form low spin heme-CO adducts. The implications for future investigations of these heme O2 and CO adducts are discussed.

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Section: Resultsmentioning

confidence: 99%

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

Sharma

Karlin

2013

Polyhedron

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“…The typical examples are cytochrome c oxidase and laccase, their active sites contain the similar metal clusters of assembled Cu 2 þ complexes 19,20 . Previous work showed that laccase in vitro is more desirable as the quasichampion potential (onset at 1.2 V versus reversible hydrogen electrode (RHE), pH ¼ 4) is observed on its modified electrode 21 , suggesting that Cu 2 þ ion is supposed to be an ideal catalytic site as long as the energy level of the d-electrons is tuned to a reasonable state.…”

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confidence: 99%

Bioinspired copper catalyst effective for both reduction and evolution of oxygen

et al. 2014

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In many green electrochemical energy devices, the conversion between oxygen and water suffers from high potential loss due to the difficulty in decreasing activation energy. Overcoming this issue requires full understanding of global reactions and development of strategies in efficient catalyst design. Here we report an active copper nanocomposite, inspired by natural coordination environments of catalytic sites in an enzyme, which catalyzes oxygen reduction/evolution at potentials closely approaching standard potential. Such performances are related to the imperfect coordination configuration of the copper(II) active site whose electron density is tuned by neighbouring copper(0) and nitrogen ligands incorporated in graphene. The electron transfer number of oxygen reduction is estimated by monitoring the redox of hydrogen peroxide, which is determined by the overpotential and electrolyte pH. An in situ fluorescence spectroelectrochemistry reveals that hydroxyl radical is the common intermediate for the electrochemical conversion between oxygen and water.

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“…The electronic and structural features of such dioxygenmetal complexes, which vary with the ligand structure, have attracted much research [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

An oxygen reduction catalytic process through superoxo adsorption states on n-type doped h-BN: A first-principles study

Shin

Thapa

Park

2015

Current Applied Physics

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Superoxo, μ-peroxo, and μ-oxo complexes from heme/O ₂ and heme-Cu/O ₂ reactivity: Copper ligand influences in cytochrome c oxidase models

Cited by 99 publications

References 46 publications

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

Bioinspired copper catalyst effective for both reduction and evolution of oxygen

An oxygen reduction catalytic process through superoxo adsorption states on n-type doped h-BN: A first-principles study

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Superoxo, μ-peroxo, and μ-oxo complexes from heme/O 2 and heme-Cu/O 2 reactivity: Copper ligand influences in cytochrome c oxidase models

Cited by 99 publications

References 46 publications

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

New heme–dioxygen and carbon monoxide adducts using pyridyl or imidazolyl tailed porphyrins

Bioinspired copper catalyst effective for both reduction and evolution of oxygen

An oxygen reduction catalytic process through superoxo adsorption states on n-type doped h-BN: A first-principles study

Contact Info

Product

Resources

About

Superoxo, μ-peroxo, and μ-oxo complexes from heme/O ₂ and heme-Cu/O ₂ reactivity: Copper ligand influences in cytochrome c oxidase models