Encapsulating Subsite analogues of the [FeFe]-hydrogenases in micelles enables direct water interactions

Research output: Contribution to journalArticle

Encapsulation of sub-site 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 sub-site analogue 1 can be tuned with micelle size, while IR spectroscopy provides a straightforward tool that can be used to measure and finetune the chemical environment of catalyst species in self-assembled structures.
Original languageEnglish
Pages (from-to)2838-2843
Number of pages6
JournalJournal of Physical Chemistry Letters
Volume7
Early online date10 Jul 2016
DOIs
StatePublished - 21 Jul 2016

    Research areas

  • [FeFe] hydrogenase, infrared spectroscopy, ultrafast infrared spectroscopy, micelle, water solubility, subsite analogues, catalytic ability, self-assembled sturctures

Bibliographical note

“This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Physical Chemistry Letters, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://dx.doi.org10.1021/acs.jpclett.6b01338

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