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Advanced applications of X-ray Absorption Spectroscopy to the study of protein metal sites.

We present a study of the metal sites of different proteins through X-ray Absorption Fine Structure (XAFS) spectroscopy. First of all, the capabilities of XAFS analysis have been improved by ab initio simulation of the near-edge region of the spectra, and an original analysis method has been proposed. The method subsequently served ad a tool to treat diverse biophysical problems, like the inhibition of proton-translocating proteins by metal ions and the matrix effect exerted on photosynthetic proteins (the bacterial Reaction Center, RC) by strongly dehydrate sugar matrices. A time-resolved study of Fe site of RC with μs resolution has been as well attempted.
Finally, a further step aimed to improve the reliability of XAFS analysis has been performed by calculating the dynamical parameters of the metal binding cluster by means of DFT methods, and the theoretical result obtained for MbCO has been successfully compared with experimental data.

Identiferoai:union.ndltd.org:unibo.it/oai:amsdottorato.cib.unibo.it:2535
Date04 May 2010
CreatorsVeronesi, Giulia <1982>
ContributorsBoscherini, Federico
PublisherAlma Mater Studiorum - Università di Bologna
Source SetsUniversità di Bologna
LanguageEnglish
Detected LanguageEnglish
TypeDoctoral Thesis, PeerReviewed
Formatapplication/pdf
Rightsinfo:eu-repo/semantics/openAccess

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