Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Lisa Olshansky"'
Autor:
Saman Fatima, David G. Boggs, Noor Ali, Peter J. Thompson, Megan C. Thielges, Jennifer Bridwell-Rabb, Lisa Olshansky
Publikováno v:
J Am Chem Soc
Many naturally occurring metalloenzymes are gated by rate-limiting conformational changes, and there exists a critical interplay between macroscopic structural rearrangements of the protein and subatomic changes affecting the electronic structure of
Autor:
Paul J. Griffin, Bronte J. Charette, John H. Burke, Josh Vura-Weis, Richard D. Schaller, David J. Gosztola, Lisa Olshansky
Publikováno v:
Journal of the American Chemical Society. 144:12116-12126
The continued development of solar energy as a renewable resource necessitates new approaches to sustaining photodriven charge separation (CS). We present a bioinspired approach in which photoinduced conformational rearrangements at a ligand are tran
Publikováno v:
Dalton Trans
The interplay between oxidation state and coordination geometry dictates both kinetic and thermodynamic properties underlying electron transfer events in copper complexes. An ability to stabilize both Cu(I) and Cu(II) oxidation states in a single con
Publikováno v:
Dalton Transactions.
The geometries of copper coordination complexes are intricately related to their electron transfer capabilities, but the role of dynamics in these processes are not fully understood. We have previously reported...
Publikováno v:
Inorg Chem
Active site hydrogen-bond (H-bond) networks represent a key component by which metalloenzymes control the formation and deployment of high-valent transition metal-oxo intermediates. We report a series of dinuclear cobalt complexes that serve as struc
Publikováno v:
Biochemistry. 59:1442-1453
Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides (NDP) to deoxynucleotides (dNDP), in part, by controlling the ratios and quantities of dNTPs available for DNA replication and repair. The active form of Escherichia coli class I
Publikováno v:
Biophysical Journal. 122:181a
Autor:
T. Don Tilley, Ariel L. Furst, Jaicy Vallapurackal, A. S. Borovik, Lisa Olshansky, Raúl Huerta-Lavorie, Andy I. Nguyen
Publikováno v:
Journal of the American Chemical Society. 140:2739-2742
Artificial metalloproteins (ArMs) containing Co4O4 cubane active sites were constructed via biotin-streptavidin technology. Stabilized by hydrogen bonds (H-bonds), terminal and cofacial CoIII-OH2 moieties are observed crystallographically in a series
Autor:
Lisa, Olshansky, Raúl, Huerta-Lavorie, Andy I, Nguyen, Jaicy, Vallapurackal, Ariel, Furst, T Don, Tilley, A S, Borovik
Publikováno v:
Journal of the American Chemical Society. 140(8)
Artificial metalloproteins (ArMs) containing Co4O4 cubane active sites were constructed via biotin-streptavidin technology. Stabilized by hydrogen bonds (H-bonds), terminal and cofacial CoIII–OH2 moieties are observed crystallographically in a seri
Publikováno v:
Biochemistry. 55(23)
The Escherichia coli class Ia ribonucleotide reductase (RNR) achieves forward and reverse proton-coupled electron transfer (PCET) over a pathway of redox active amino acids (β-Y122 ⇌ β-Y356 ⇌ α-Y731 ⇌ α-Y730 ⇌ α-C439) spanning ∼35 Å a