Search results for "Heme proteins"
showing 4 items of 4 documents
A Versatile and Convenient Method for the Functionalization of Porphyrins
2001
International audience; The condensation of 3-(chloromethyl)benzoyl chloride with different atropisomers of meso-(tetra-o-aminophenyl)porphyrin (TAPP), followed by the reaction of a series of nucleophilic reagents leads, among others, to precursors of biomimetic models of heme proteins such as cytochrome c oxidase (CcO). This synthesis can also be applied as an efficient two-step reaction to obtain highly functionalized porphyrin derivatives potentially useful for cation binding.
Application of 3-Quinolinoyl Picket Porphyrins to the Electroreduction of Dioxygen to Water: Mimicking the Active Site of Cytochromec Oxidase
2001
International audience
Protein dynamics: conformational disorder, vibrational coupling and anharmonicity in deoxy-hemoglobin and myoglobin.
1993
In this work we study the temperature dependence of the Soret band lineshape of deoxymyoglobin and deoxyhemoglobin, in the range 300-20 K. To fit the measured spectra we use an approach originally proposed by Champion and coworkers (Srajer et al. 1986; Srajer and Champion 1991). The band profile is modelled as a Voigt function that accounts for the coupling with low frequency vibrational modes, whereas the coupling with high frequency modes is responsible for the vibronic structure of the spectra. Moreover, owing to the position of the iron atom out of the mean heme plane, inhomogeneous broadening brings about a non-Gaussian distribution of 0-0 electronic transition frequencies. The reporte…
Immobilization of proteins in silica gel: Biochemical and biophysical properties
2015
The development of silica-based sol-gel techniques compatible with the retention of protein structure and function started more than 20 years ago, mainly for the design of biotechnological devices or biomedical applications. Silica gels are optically transparent, exhibit good mechanical stability, are manufactured with different geometries, and are easily separated from the reaction media. Biomolecules encapsulated in silica gel normally retain their structural and functional properties, are stabilized with respect to chemical and physical insults, and can sometimes exhibit enhanced activity in comparison to the soluble form. This review briefly describes the chemistry of protein encapsulat…