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

Fritzsch, Robby, Brady, Owen, Adair, Elaine, Wright, Joseph A., Pickett, Christopher J. and Hunt, Neil T. (2016) Encapsulating subsite analogues of the [FeFe]-hydrogenases in micelles enables direct water interactions. The Journal of Physical Chemistry Letters, 7 (14). pp. 2838-2843. ISSN 1948-7185

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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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Related URLs:
Depositing User: Pure Connector
Date Deposited: 24 Sep 2016 01:12
Last Modified: 09 Apr 2019 11:24
URI: https://ueaeprints.uea.ac.uk/id/eprint/59909
DOI: 10.1021/acs.jpclett.6b01338

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