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

 
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1992 (EN)
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 (EN)

Gerothanassis, I. P. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Gerothanassis, I. P. (EN)

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. (EN)

hemoglobin cooperativity (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Journal of the Chemical Society-Chemical Communications (EN)

English

1992

<Go to ISI>://A1992HQ25100006

Royal Society of Chemistry (EN)



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