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From the same journal

Encapsulating Subsite Analogues of the [FeFe]-Hydrogenases in Micelles Enables Direct Water Interactions

Research output: Contribution to journalArticle

Author(s)

  • Robby Fritzsch
  • Owen Brady
  • Elaine Adair
  • Joseph A. Wright
  • Christopher J. Pickett
  • Neil T. Hunt

Department/unit(s)

Publication details

JournalJOURNAL OF PHYSICAL CHEMISTRY LETTERS
DatePublished - 21 Jul 2016
Issue number14
Volume7
Number of pages6
Pages (from-to)2838-2843
Original languageEnglish

Abstract

Encapsulation of subsite analogues of the [FeFe]-hydrogenase enzymes in supramolecular structures has been shown to dramatically increase their catalytic ability, but the molecular basis for this enhancement remains unclear. We report the results of experiments employing infrared absorption, ultrafast infrared pump-probe, and 2D-IR spectroscopy to investigate the molecular environment of Fe2(pdt)(CO)6 (pdt: propanedithiolate) [1] encapsulated in the dispersed alkane phase of a heptane-dodecyltrimethylammonium bromide-water microemulsion. It is demonstrated that 1 is partitioned between two molecular environments, one that closely resembles bulk heptane solution and a second that features direct hydrogen-bonding interactions with water molecules that penetrate the surfactant shell. Our results demonstrate that the extent of water access to the normally water-insoluble subsite analogue 1 can be tuned with micelle size, while IR spectroscopy provides a straightforward tool that can be used to measure and fine-tune the chemical environment of catalyst species in self-assembled structures.

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