Results 241 to 250 of about 80,355 (300)

Live Imaging of Silver Nanostructures Electrochemically Dissolving at Open-Circuit Potential. [PDF]

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Körner A, Morales AL, Fritsch B, Fiedler L, Mulvey JT, Göllner C, Alloyeau D, Patterson JP, Malgaretti P, Mayrhofer KJJ, Cherevko S, Hutzler A.   +11 more
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Bipolar electrochemical tweezers using pristine carbon fibers with intrinsically asymmetric features. [PDF]

Nat Commun
Gupta B, Shrivastav V, Sundriyal S, Melvin AA, Holdynski M, Kuhn A, Nogala W.   +6 more
europepmc   +1 more source

Dissecting Bioelectrical Networks in Photosynthetic Membranes with Electrochemistry. [PDF]

J Am Chem Soc
Lawrence JM, Egan RM, Wey LT, Bali K, Chen X, Kosmützky D, Eyres M, Nan L, Wood MH, Nowaczyk MM, Howe CJ, Zhang JZ.   +11 more
europepmc   +1 more source

On the Rise of Slurry Electrolysis for Energy Applications. [PDF]

Chem Asian J
Xiong J, Lian G, Chen Z.
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Tunable stereoselectivity in a wireless electrochemical microreactor using natural chiral ionic liquids.

Green Chem
Grecchi S, Mezzetta A, Guazzelli L, Arnaboldi S.   +3 more
europepmc   +1 more source

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Direct electrochemistry of photosystem I

Journal of Electroanalytical Chemistry, 2001
Abstract Direct electrochemistry has been developed into a powerful tool for the analysis of soluble proteins and enzymes over the past two decades. In the present study, we have expanded the range of proteins to include a solubilized membrane protein, photosystem I.
Olaf Kievit, Gary W Brudvig
openaire   +1 more source

Direct electrochemistry of pentachlorophenol hydroxylase

SPIE Proceedings, 2001
The direct electrochemistry of flavin-containing monooxygenase, pentachlorophenol hydroxlase (PCPH), has been investigated under a variety of conditions. PCPH underwent a two-electron process on the electrodes, which correspond to the reduction/oxidation of FAD/FADH2 within the enzyme. The electrochemical response of PCPH relies on the interface of the
Wei-hong Xie, H. Allen, O. Hill, Luet L. Wong   +3 more
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Direct Electrochemistry of a Bacterial Sulfite Dehydrogenase

Journal of the American Chemical Society, 2002
Sulfite dehydrogenase from Starkeya novella is an alphabeta heterodimer comprising a 40.6 kDa subunit (containing the Mo cofactor) and a smaller 8.8 kDa heme c subunit. The enzyme catalyses the oxidation of sulfite to sulfate with the natural electron acceptor being cytochrome c550.
Aguey-Zinsou, Kondo-Francois, Bernhardt, Paul. V., Kappler, Ulrike, McEwan, Alastair G.   +3 more
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