http://www.cnr.it/ontology/cnr/individuo/prodotto/ID3535
Cloning, expression and physicochemical characterization of a di-heme cytochrome c(4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125 (Articolo in rivista)
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- Cloning, expression and physicochemical characterization of a di-heme cytochrome c(4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125 (Articolo in rivista) (literal)
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- 2008-01-01T00:00:00+01:00 (literal)
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Di Rocco, G; Battistuzzi, G; Borsari, M; De Rienzo, F; Ranieri, A; Tutino, ML; Sola, M (2008)
Cloning, expression and physicochemical characterization of a di-heme cytochrome c(4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125
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- Di Rocco, G; Battistuzzi, G; Borsari, M; De Rienzo, F; Ranieri, A; Tutino, ML; Sola, M (literal)
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- \"[Di Rocco, Giulia; Battistuzzi, Gianantonio; Borsari, Marco; De Rienzo, Francesca; Ranieri, Antonio; Sola, Marco] Univ Modena & Reggio Emilia, Dept Chem, I-41100 Modena, Italy; [De Rienzo, Francesca; Sola, Marco] Natl Ctr nanoStruct & bioSyst Surfaces, CNR, INFM, I-41100 Modena, Italy; [Tutino, Maria Luisa] Univ Naples Federico 2, Dipartimento Chim Organ & Biochim, I-80126 Naples, Italy (literal)
- Titolo
- Cloning, expression and physicochemical characterization of a di-heme cytochrome c(4) from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125 (literal)
- Abstract
- The 20-kDa di-heme cytochrome c(4) from the psycrophilic bacterium Pseudoalteromonas haloplanktis TAC 125 was cloned and expressed in Escherichia coli and investigated through UV-vis and H-1 NMR spectroscopies and protein voltammetry. The model structure was computed using the X-ray structure of Pseudomonas stutzeri cytochrome c(4) as a template. The protein shows unprecedented properties within the cytochrome c(4) family, including (1) an almost nonpolar surface charge distribution, (2) the absence of high-spin heme Fe(III) states, indicative of a thermodynamically stable and kinetically inert axial heme His,Met coordination, and (3) identical E degrees' values for the two heme centers (+0.322 V vs the standard hydrogen elecrode). At pH extremes, both heme groups undergo the 'acid' and 'alkaline' conformational transitions typical of class I cytochromes c, involving ligand-exchange equilibria, whereas at intermediate pH values their electronic properties are sensitive to several residue ionizations. (literal)
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