Scozzafava Andrea

Professore Ordinario

Farmacia

CHIMICA

C03

Cognome e Nome

BRIGANTI FABRIZIO

Qualifica

P.A.

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

FERRARONI MARTA

Qualifica

RICERCATORE CONFERMATO

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

RANDAZZO DEMETRIO

Qualifica

TECNICO

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

SCOZZAFAVA ANDREA

Qualifica

P.O.

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

TILLI SILVIA

Qualifica

TECNICO

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

ALESSANDRO CECCHI

Qualifica

DOTTORANDO

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

ALESSIO INNOCENTI

Qualifica

ASSEGNISTA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

ANTONELLA GULLOTTO

Qualifica

DOTTORANDA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

CLAUDIA TEMPERINI

Qualifica

ASSEGNISTA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

DANIELA VULLO

Qualifica

ASSEGNISTA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

ILARIA CIULLINI

Qualifica

DOTTORANDA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

IRENE MATERA

Qualifica

ASSEGNISTA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

Cognome e Nome

SUPURAN CLAUDIU

Qualifica

ASSEGNISTA

Dipartimento

CHIMICA

Ente di appartenenza

UNIVERSITA’ di FIRENZE

The research unit is involved in the structure-function characterization of metalloenzymes. In particular two distinct research lines are active which are related to metalloenzymes involved in biodegradative processes or in human diseases. With reference to the first topic new ring opening dioxygenases and mushroom laccases have been characterized. Regarding the biomedical area, the studied enzymes have been in particular carbonic anhydrase and some metalloproteases. The research unit, beside expressing and isolating new enzymes is also capable to determine their three-dimensional structure through X ray diffraction studies, as well as of synthesizing new molecules which can act as inhibitors or activators of the enzymes. Very many papers have been published regarding the synthesis and characterization of these inhibitors/activators and the structures of the enzyme/inhibitor(activator) adducts. In many cases the new molecules have properties such to be used as potential drugs. In particular carbonic anhydrase inhibitors can be used for the treatment of glaucoma, obesity and for diagnostic purposes at the very early stage of development of malignant tumors i.e. Kidney tumors. In the case of industrial application of degradative enzymes new approaches have been developed though the use of micellar systems which enhance the activity of native or engineerized microorganisms toward hydrophobic substrates . In this manner it is possible for example to accelerate the degradation of the substrate (bioremediation purposes) or to obtain intermediates with high added value from the substrates (an example of “green chemistry” through an enzymatic approach). The research unit has fruitful scientific collaborations with many excellent European and non European research institutions.

Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. (2005) 280, 21144-54 Ferraroni M, Seifert J, Travkin VM, Thiel M, Kaschabek S, Scozzafava A, Golovleva L, Schlomann M, Briganti F.

Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP. J. Biol. Chem. (2004) 279, 27646-55 Ferraroni M, Solyanikova IP, Kolomytseva MP, Scozzafava A, Golovleva L, Briganti F.

Efficient polycyclic aromatic hydrocarbons dihydroxylation in direct micellar systems. Biotech. Bioeng. (2001) 74, 240-8 Randazzo D, Berti D, Briganti F, Baglioni P, Scozzafava A, Di Gennaro P, Galli E, Bestetti G.

Hypoxia activates the capacity of tumor-associated carbonic anhydrase IX to acidify extracellular pH. FEBS Lett. (2004) 577, 439-45. Svastova E, Hulikova A, Rafajova M, Zat'ovicova M, Gibadulinova A, Casini A, Cecchi A, Scozzafava A, Supuran CT, Pastorek J, Pastorekova S.

Carbonic anhydrase inhibitors. The mitochondrial isozyme VB as a new target for sulfonamide and sulfamate inhibitors. J. Med. Chem. (2005) 48, 7860-6. Nishimori I, Vullo D, Innocenti A, Scozzafava A, Mastrolorenzo A, Supuran CT.

Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II. J. Med. Chem. (2005) 48, 5271-7. Menchise V, De Simone G, Alterio V, Di Fiore A, Pedone C, Scozzafava A, Supuran CT.

Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition. J. Med. Chem. (2004) 47, 550-7 Weber A, Casini A, Heine A, Kuhn D, Supuran CT, Scozzafava A, Klebe G.

Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family. J Biol. Chem. (2004) 279, 2719-27 Lehtonen J, Shen B, Vihinen M, Casini A, Scozzafava A, Supuran CT, Parkkila AK, Saarnio J, Kivela AJ, Waheed A, Sly WS, Parkkila S.

Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: molecular and X-ray crystallographic studies. Biochemistry (2003), 42, 9013-21 De Simone G, Menchise V, Omaggio S, Pedone C, Scozzafava A, Supuran CT.

Carbonic anhydrase inhibitors. Med. Res. Rev. (2003) 23, 146-89 Supuran CT, Scozzafava A, Casini A.