PENNATI, ANDREA
PENNATI, ANDREA
DIPARTIMENTO DI SCIENZE BIOMOLECOLARI E BIOTECNOLOGIE (attivo dal 01/06/2003 al 27/04/2012)
Ingested microscopic plastics translocate from the gut cavity of juveniles of the ascidian Ciona intestinalis
2019 S. Messinetti, S. Mercurio, G. Scari, A. Pennati, R. Pennati
The ferredoxin-NADP+ reductase/ferredoxin electron transfer system of Plasmodium falciparum
2009 E. Balconi, A. Pennati, D. Crobu, V. Pandini, R. Cerutti, G. Zanetti, A. Aliverti
Role of residues Asp161, Arg164 and Glu211 in Mycobacterium tuberculosis NADPH-ferredoxin reductase
2008 F. Ciriello, P. Vella, A. Pennati, V. Pandini, G. Zanetti, A. Aliverti
Effect of salt and pH on the reductive half-reaction of Mycobacterium tuberculosis FprA with NADPH
2008 A. Pennati, G. Zanetti, A. Aliverti, G. Gadda
Structural and functional diversity of ferredoxin-NADP+ reductases
2008 A. Aliverti, V. Pandini, A. Pennati, M. de Rosa, G. Zanetti
Enzymatic oxidation of NADP+ to its 4-oxo derivative is a side-reaction displayed only by the adrenodoxin reductase type of ferredoxin-NADP+ reductases
2007 M. De Rosa, A. Pennati, V. Pandini, E. Monzani, G. Zanetti, A. Aliverti
Analysis by protein engineering , rapid kinetics and X-ray crystallography of the reductive half-reaction catalyzed by FprA, a Mycobacterium tuberculosis homologue of adrenodoxin reductase
2006 A. Aliverti, A. Pennati, A. Razeto, M. de Rosa, R. Cerutti, V. Pandini, A. Mattevi, M.A. Vanoni, G. Zanetti
Probing the catalytic mechanism of Mycobacterium tuberculosis NADPH-ferredoxin reductase by protein engineering, rapid kinetics and X-ray crystallography
2006 A. Pennati
The unusual NADP+ oxidase activity of flavoenzymes belonging to the adrenodoxin reductase family
2006 M. De Rosa, C. D'Angiò, A. Pennati, A. Aliverti, G. Zanetti
The unusual NADP+ oxidase activity of flavoenzymes belonging to the adrenodoxin reductase family
2006 M. De Rosa, C. D'Angiò, A. Pennati, A. Aliverti, G. Zanetti
Functional characterization of Plasmodium falciparum ferredoxin-NADP+ reductase
2006 E. Balconi, A. Pennati, E. Grassi, V. Pandini, F. Seeber, A. Aliverti, G. Zanetti
Hydride transfer between pyridine nucleotide and FAD in Mycobacterium tuberculosis FprA: role of the invariant His57 in catalysis as studied by protein engineering, stopped-flow kinetics and X-ray crystallography
2006 A. Pennati, A. Razeto, M. de Rosa, R. Cerutti, V. Pandini, M.A. Vanoni, A. Mattevi, A. Aliverti, G. Zanetti
Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA
2006 A. Pennati, A. Razeto, M. de Rosa, V. Pandini, M.A. Vanoni, A. Mattevi, A. Coda, A. Aliverti, G. Zanetti
Role of the catalytic dyad His57-Glu214 in FprA, a Mycobacterium tuberculosis homolog of adrenodoxin reductase
2005 A. Pennati, M. de Rosa, V. Pandini, A. Aliverti, G. Zanetti
A new catalytic activity of the NADPH-ferredoxin reductase of Mycobacterium tuberculosis
2005 M. de Rosa, C.F. D'Angio', A. Pennati, A. Aliverti, G. Zanetti
The role of the active-site residues His57 and Glu214 of FprA, a Mycobacterium tuberculosis homolog of adrenodoxin reductase
2005 A. Aliverti, A. Pennati, V. Pandini, M.A. Vanoni, G. Zanetti
The role of the active-site residues His57 and Glu214 of Mycobacterium tuberculosis FprA
2005 A. Aliverti, A. Pennati, M. De Rosa, V. Pandini, M.A. Vanoni, G. Zanetti