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Myoglobin resonance Raman spectroscopy

A variety of physical methods has been used to ascertain whether or not surface ruthenation alters the structure of a protein. UV-vis, CD, EPR, and resonance Raman spectroscopies have demonstrated that myoglobin [14, 18], cytochrome c [5, 16, 19, 21], and azurin [13] are not perturbed structurally by the attachment of a ruthenium complex to a surface histidine. The reduction potential of the metal redox center of a protein and its temperature dependence are indicators of protein structure as well. Cyclic voltammetry [5, 13], differential pulse polarography [14,21], and spectroelectrochemistry [12,14,22] are commonly used for the determination of the ruthenium and protein redox center potentials in modified proteins. [Pg.111]

A variety of additional measurements have been made on the photolysis behavior of myoglobin and the related protein, hemoglobin. These include room-temperature transient electronic absorption studies in the nanosecond range,521 nanosecond-to-picosecond resonance Raman spectroscopy,522,523 and low-temperature transient electronic absorption measurements in regions other than the Soret band.524... [Pg.224]

Feitelson, J. and Spiro, T. G. 1986, Bonding in zinc proto- and mesoporphyrin substituted myoglobin and model compounds studied by resonance raman spectroscopy. Inorganic Chemistry 25, 861-865. [Pg.392]

Mizutani, Y Kitagawa, T., Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy. Chem. Rec. 2001,1, 258-275. [Pg.224]

Gao, Y El-Mashtoly, S. F. Pal, B. Hayashi, T Harada, K. Kitagawa, T., Pathway of information transmission from heme to protein upon ligand binding/dissociation in myoglobin revealed by UV resonance Raman spectroscopy. J. Biol. Chem. 2006, 281,24637-24646. [Pg.224]

Sitter AJ, Reczek CM, Temer J (1985) Observation of the Fe -0 stretching vibration of ferryl myoglobin by resonance Raman spectroscopy. Biochimica Et Biophysica Acta (BBA) Protein Struct Mol Enzymol 828 229-235... [Pg.162]

Sato, A., Mizutani, Y. Picosecond structural dynamics of myoglobin following photodissociation of carbon monoxide as revealed by ultraviolet time-resolved resonance Raman spectroscopy. Biochemistry 44, 14709-14714 (2005)... [Pg.545]

A.R. Bizzarri, S. Cannistraro, Surface-enhanced resonance Raman spectroscopy signals from single myoglobin molecules. Appl. Spectrosc. 56, 1531 (2002)... [Pg.120]

T.M. Cotton, The applications of SERS to biological systems, in Spectroscopy of Surfaces, ed. by R.J.H. Clark, R.E. Hester (Wiley Sons, Chichester, 1988), pp. 90-153 T.M. Cotton, S.G. Schultz, R.P. Van Duyne, Surface-enhanced resonance Raman scattering from cytochrome c and myoglobin adsorbed on a sUvct electrode. J. Am. Chem. Soc. 102, 7960 (1980)... [Pg.121]

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See also in sourсe #XX -- [ Pg.48 , Pg.437 , Pg.483 , Pg.483 , Pg.487 ]



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