Search Results - (Author, Cooperation:G. M. Giacometti)
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1L. Carraretto ; E. Formentin ; E. Teardo ; V. Checchetto ; M. Tomizioli ; T. Morosinotto ; G. M. Giacometti ; G. Finazzi ; I. Szabo
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-09-07Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Light ; *Photosynthesis ; Potassium Channels/genetics/*metabolism ; Potassium Channels, Tandem Pore Domain/genetics/*metabolism ; Recombinant Proteins/genetics/metabolism ; Thylakoids/*metabolism/ultrastructurePublished by: -
2Bianconi, A. ; Congiu-Castellano, A. ; Giovannelli, A. ; Dell'Ariccia, M. ; Burattini, E. ; Durham, P. J. ; Giacometti, G. M.
Springer
Published 1986Staff ViewISSN: 1432-1017Keywords: Myoglobin ; XANES ; synchrotron radiation ; protein structureSource: Springer Online Journal Archives 1860-2000Topics: BiologyPhysicsNotes: Abstract The ligand bonding geometry of carboxy-and cyanomet-myoglobin (MbCO and MbCN) has been measured by the XANES method (X-ray Absorption Near Edge Structure). A comparison between the ligand bonding geometry of carboxy- and cyanomet-myoglobin and of chelated protoheme methyl ester shows that the bent Fe−C−O configuration is the same in both systems. Therefore, we suggest that this configuration is not associated with any steric contraint imposed by the side chains of the aminoacid residues at the distal side of the heme pocket.Type of Medium: Electronic ResourceURL: