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

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

[img]
Preview
Text (Fritzsch-etal-JPCL2016-Encapsulating-Subsite-analogues-of-the-[FeFe]-hydrogenases)
Fritzsch_etal_JPCL2016_Encapsulating_Subsite_analogues_of_the_FeFe_hydrogenases.pdf
Accepted Author Manuscript

Download (544kB)| Preview

    Abstract

    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.