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Katherine A. Brown

Researcher at National Renewable Energy Laboratory

Publications -  29
Citations -  2240

Katherine A. Brown is an academic researcher from National Renewable Energy Laboratory. The author has contributed to research in topics: Electron transfer & Nanoparticle. The author has an hindex of 16, co-authored 28 publications receiving 1850 citations. Previous affiliations of Katherine A. Brown include Massachusetts Institute of Technology.

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Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid.

TL;DR: It is shown that cadmium sulfide (CdS) nanocrystals can be used to photosensitize the nitrogenase molybdenum-iron (MoFe) protein, where light harvesting replaces ATP hydrolysis to drive the enzymatic reduction of N2 into NH3.
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Characterization of Photochemical Processes for H2 Production by CdS Nanorod–[FeFe] Hydrogenase Complexes

TL;DR: This paper explored the effects of the CdS:CaI molar ratio, sacrificial donor concentration, and light intensity on photocatalytic H(2) production, which were interpreted on the basis of contributions to electron transfer, hole transfer, or rate of photon absorption, respectively.
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Controlled assembly of hydrogenase-CdTe nanocrystal hybrids for solar hydrogen production.

TL;DR: Nc-CdTe and H(2)ase spontaneously assemble into complexes that upon illumination transfer photogenerated electrons from core nc- CdTe states to H(1)ase, with low H( 2)ase coverages promoting optimal orientations for intramolecular ET and solar H(3) production.
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Electron Transfer Kinetics in CdS Nanorod–[FeFe]-Hydrogenase Complexes and Implications for Photochemical H2 Generation

TL;DR: The intricate kinetic pathways involved in photochemical H2 generation in CdS-CaI complexes are discussed, and it is proposed that gains in efficiencies of H2 production could be achieved by increasing k(ET) and/or decreasing k(CdS) through structural modifications of the nanocrystals.
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Catalytic Turnover of [FeFe]-Hydrogenase Based on Single-Molecule Imaging

TL;DR: Electrochemical and single-molecule imaging studies carried out on a catalytically active hydrogenase preparation revealed uniform surface coverage with sufficient stability to undergo repeated scanning with a STM tip as well as other electrochemical investigations.