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DOI: 10.5445/IR/1000044644
Originalveröffentlichung
DOI: 10.12688/f1000research.5836.1

Fourier transform infrared spectroscopy study of ligand photodissociation and migration in inducible nitric oxide synthase

Horn, M.; Nienhaus, K.; Nienhaus, G.U.

Abstract:
Inducible nitric oxide synthase (iNOS) is a homodimeric heme enzyme that catalyzes the formation of nitric oxide (NO) from dioxygen and L-arginine (L-Arg) in a two-step process. The produced NO can either diffuse out of the heme pocket into the surroundings or it can rebind to the heme iron and inhibit enzyme action. Here we have employed Fourier transform infrared (FTIR) photolysis difference spectroscopy at cryogenic temperatures, using the carbon monoxide (CO) and NO stretching bands as local probes of the active site of iNOS. Characteristic changes were observed in the spectra of the heme-bound ligands upon binding of the cofactors. Unlike photolyzed CO, which becomes trapped in well-defined orientations, as indicated by sharp photoproduct bands, photoproduct bands of NO photodissociated from the ferric heme iron were not visible, indicating that NO does not reside in the protein interior in a well-defined location or orientation. This may be favorable for NO release from the enzyme during catalysis because it reduces self-inhibition. Moreover, we used temperature derivative spectroscopy (TDS) with FTIR monitoring to explore the ... mehr


Zugehörige Institution(en) am KIT Institut für Angewandte Physik (APH)
Publikationstyp Zeitschriftenaufsatz
Jahr 2014
Sprache Englisch
Identifikator ISSN: 2046-1402
URN: urn:nbn:de:swb:90-446446
KITopen ID: 1000044644
Erschienen in Faculty of 1000 Research
Band 3
Seiten 290/1-13
Bemerkung zur Veröffentlichung Gefördert durch den KIT-Publikationsfonds
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