Structural Differences of the Iron Dioxygen Moiety of Hemoprotein Models with and without an Axial Hindered Base as Revealed by O-17 Nmr and Ftir Spectroscopy in Solution (Journal article)

Gerothanassis, I. P./ Loock, B./ Momenteau, M.


The N-H stretching vibrations of the oxygenated 'hybrid' haemoprotein models with an axial hindered base indicate that there is no conventional hydrogen bond with the terminal oxygen of the Fe-O2 moiety, contrary to the models with an axial unhindered base; however, the Fe-O2 moiety is highly polarizable as indicated by O-17 NMR spectroscopy.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: hemoglobin cooperativity,oxygen-binding,carbon-monoxide,t-state,porphyrins,bond,hemoproteins,coordination,systems
URI: http://olympias.lib.uoi.gr/jspui/handle/123456789/9276
ISSN: 0022-4936
Link: <Go to ISI>://A1992HQ25100006
http://pubs.rsc.org/en/Content/ArticleLanding/1992/C3/c39920000598
Publisher: Royal Society of Chemistry
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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