Investigation of amino acid containing [FeFe] hydrogenase models concerning pendant base effects

Author(s)
Ulf-Peter Apfel, Christian Kowol, Yvonne Halpin, Florian Kloss, Joachim Kübel, Helmar Görls, Johannes G. Vos, Bernhard Keppler, Enrico Morera, Gino Lucente, Wolfgang Weigand
Abstract

The present investigations deal with the modeling of the peptide surrounding of [FeFe] hydrogenase using amine containing disulphides to simulate possible influences of the amino acid lysine (K237) on the electrochemical and electrocatalytic properties of biomimetic compounds based on [Fe2S2] moieties. Fe3(CO)12 was reacted with Boc-4-amino-1,2-dithiolane, Boc-Adt-OMe (Adt = 4-amino-1,2-dithiolane-4-carboxylic acid, Boc = tert-butoxycarbonyl) and Boc-Adp tert-butyl ester (Adp = (S)-2-amino-3-(1,2-dithiolan-4-yl)propionic acid) to elongate the Fe?N distance in comparison to the well known [Fe2{(SCH2)2NR}(CO)6] model complexes. Efforts to deprotect the complexes containing Boc-4-amino-1,2-dithiolane with trifluoroacetic acid result in the formation of [Fe3(?3-O)(?-O2C2F3)6(OC4H8)2(H2O)]. The novel [2Fe2S] complexes are characterized using spectroscopic, electrochemical techniques and X-ray diffraction studies.

Organisation(s)
Department of Inorganic Chemistry
External organisation(s)
Friedrich-Schiller-Universität Jena, Dublin City University, Sapienza University of Rome
Journal
Journal of Inorganic Biochemistry
Volume
103
Pages
1236-1244
No. of pages
9
ISSN
0162-0134
DOI
https://doi.org/10.1016/j.jinorgbio.2009.07.005
Publication date
2009
Peer reviewed
Yes
Austrian Fields of Science 2012
104003 Inorganic chemistry, 301305 Medical chemistry, 104002 Analytical chemistry
Portal url
https://ucrisportal.univie.ac.at/en/publications/83a80180-c4d5-44b9-9620-e38d81ea32fb