Synthesis, Excited-State Dynamics, and Reactivity of a Directly-Linked Pyromellitimide−(Porphinato)zinc(II) Complex

Redmore, Naomi P.; Rubtsov, Igor V.; Therien, Michael J.

doi:10.1021/ic0108641

Cited by 32 publications

(38 citation statements)

References 37 publications

(78 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…With respect to the PZnPI dynamics determined in DMSO (τ CS = 1.2 ps, τ CR = 4.6 ps), note that these time constants not only resemble those previously evaluated in CH 2 Cl 2 , 27 but also those determined for a closely related PZnPI structure examined in THF (τ CS = 2.6 ps, τ CR = 9.1 ps) and DMF (τ CS = 1.8 ps, τ CR = 3.1 ps) solvents. 38 …”

Section: Resultssupporting

confidence: 70%

“…27 Similarly, the excited state dynamics evinced by PZnPI within the SAP2N peptide or in DMSO solvent display the spectroscopic hallmarks of CS state formation (PI •− , sharp absorption at ~710 nm, 35 PZn •+ , broad absorption at ~450 nm and ~700–750 nm). 27, 36,37 …”

Section: Resultsmentioning

confidence: 97%

“…Note that the general features of these transient absorption spectra resemble those elucidated previously for PZnPI in CH 2 Cl 2 solvent. 13,27 Electronic excitation of PZnPI produces a porphyrin-localized singlet excited state, 1 (PZn)*-PI, which in CH 2 Cl 2 solvent undergoes a charge separation (CS) reaction characterized by a sub ps time constant (τ CS = 770 fs), and a correspondingly rapid thermal charge recombination (CR) reaction (τ CR = 5.2 ps). 27 Similarly, the excited state dynamics evinced by PZnPI within the SAP2N peptide or in DMSO solvent display the spectroscopic hallmarks of CS state formation (PI •− , sharp absorption at ~710 nm, 35 PZn •+ , broad absorption at ~450 nm and ~700–750 nm).…”

Section: Resultsmentioning

confidence: 99%

“…The CR time constant determined for the SAP2N holo peptide, interestingly, is of similar magnitude to that evaluated for PZnPI in toluene solvent (τ CR = 91 ps), consistent with the typically low dielectric strength of the peptide interior (ε toluene = 2.38; 39 ε peptide interior ~2 – 4), 40, 41 and the expectation that a decrease in solvent polarity will augment PZn •+ PI •− charge-separated lifetime, consistent with previous studies and CR thermodynamics that underscore that this process lies in the Marcus inverted region. 27,38 …”

Section: Resultsmentioning

confidence: 99%

“…27 The molecular structure of PZnPI, and a schematic representation of SAP2 peptide and SAP2-PZnPI peptide-chromophore complex are shown in Scheme 1b and c, respectively. The detergent n -octyl- β -D-glucopyranoside (OG) was purchased from Anatrace (Maumee, OH, USA).…”

Section: Methodsmentioning

confidence: 99%

See 4 more Smart Citations

Acentric 2-D Ensembles of D-br-A Electron-Transfer Chromophores via Vectorial Orientation within Amphiphilic n-Helix Bundle Peptides for Photovoltaic Device Applications

et al. 2012

Self Cite

View full text Add to dashboard Cite

We show that simply designed amphiphilic 4-helix bundle peptides can be utilized to vectorially-orient a linearly-extended Donor-bridge-Acceptor (D-br-A) electron transfer (ET) chromophore within its core. The bundle’s interior is shown to provide a unique solvation environment for the D-br-A assembly not accessible in conventional solvents, and thereby control the magnitudes of both light-induced ET and thermal charge recombination rate constants. The amphiphilicity of the bundle’s exterior was employed to vectorially-orient the peptide-chromophore complex at a liquid-gas interface, and its ends tailored for subsequent covalent attachment to an inorganic surface, via a “directed assembly” approach. Structural data, combined with evaluation of the excited state dynamics exhibited by these peptide-chromophore complexes, demonstrates that densely-packed, acentrically ordered 2-D monolayer ensembles of such complexes at high in-plane chromophore densities approaching 1/200Å2 offer unique potential as active layers in binary heterojucntion photovoltaic devices.

show abstract

Section: Resultssupporting

confidence: 70%

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Acentric 2-D Ensembles of D-br-A Electron-Transfer Chromophores via Vectorial Orientation within Amphiphilic n-Helix Bundle Peptides for Photovoltaic Device Applications

et al. 2012

Self Cite

View full text Add to dashboard Cite

show abstract

Iron Porphyrin Chemistry

Walker¹,

Simonis²

2005

Encyclopedia of Inorganic Chemistry

View full text Add to dashboard Cite

This article reviews most aspects of the chemistry of iron porphyrins, from Fe(0) to Fe(V), including occurrence and roles of natural iron porphyrins (hemes) and their synthetic analogs, structures and electron configurations of iron porphyrins of all oxidation and spin states, π electron configuration of the porphyrin ring, synthesis of metal‐free porphyrins and other related macrocycles, insertion of iron into free‐base porphyrins and related macrocycles, the properties, reactions, uses and biological relevance of iron(0), ‐(I), ‐(II) porphyrins (the latter with S = 0, 1, and 2 spin state possibilities), of iron(II) porphyrin π‐cation radicals, of iron(III) porphyrins (with S = 1/2, 3/2, and 5/2 spin state possibilities), of iron(III) porphyrin and corrole π‐cation radicals, of iron(IV) porphyrins (including five‐ and six‐coordinate ferryl (FeO) 2+ , iron(IV) phenyl, carbene and hydrazine complexes, and the bis‐methoxide complex) and a comparison of iron(IV) porphyrins to iron(III) porphyrin π‐cation radicals, of iron(IV) porphyrin π‐cation radicals, and of the possible existence of iron(V) porphyrins. Included in the Fe(II) part are sections on addition of ligands to four‐coordinate iron(II) porphyrins, including equilibrium binding constants, photodissociation of ligands from PFeL 2 complexes, binding of small molecules (O 2 , CO, NO, HNO) to 5‐coordinate iron(II) porphyrins and design of porphyrin ligands that will mimic the active sites of heme proteins such as myoglobin and hemoglobin, the cytochromes P450 and nitric oxide synthases, and the nitrophorins and guanylyl cyclases. Included in the iron(III) part are sections on both 5‐ and 6‐coordinate high‐spin complexes and their similarities and differences, bridged or through‐space magnetically coupled complexes of high‐spin iron(III) porphyrins with other metal complexes as possible models for cytochrome oxidase and the assimilatory sulfite reductases, coupled oxidation of hemes by hydrogen peroxide or its equivalent, and the relationship of this reactivity to the reactions of heme oxygenase, iron(III) porphyrins as reduction catalysts, and photochemistry of iron(III) porphyrins, possible electron configurations of low‐spin iron(III) porphyrins, the phenomenon and possible electronic consequences of ruffling of the porphinato core in iron(III) porphyrins, the preferred orientation of planar axial ligands bound to low‐spin iron(III) porphyrins, NO complexes of iron(III) porphyrins, reduction potentials, equilibrium constants and rates of axial‐ligand addition and exchange, kinetics of axial‐ligand rotation and porphyrin ring inversion, kinetics of reduction and autoreduction of iron(III) porphyrins, electron self‐exchange between low‐spin iron(III) and iron(II) porphyrins, synthetic ferriheme proteins, and synthesis of five‐coordinate low‐spin iron(III) porphyrins having σ‐alkyl or σ‐aryl groups as axial ligands. The iron(IV) and iron(IV) cation radical sections discuss the high‐valent states of cytochromes P450 and related enzymes.

show abstract