Methotrexate and folate binding to dihydrofolate reductase. Separate characterization of the pteridine and p-aminobenzoyl binding sites by resonance Raman spectroscopy

Biochemistry ◽  
1981 ◽  
Vol 20 (11) ◽  
pp. 3219-3225 ◽  
Author(s):  
Y. Ozaki ◽  
R. W. King ◽  
P. R. Carey
Keyword(s):  
Raman Spectroscopy ◽  
Dihydrofolate Reductase ◽  
Binding Sites ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy

Biochemistry ◽  
1990 ◽  
Vol 29 (43) ◽  
pp. 10135-10140 ◽  
Author(s):  
Randy W. Larsen ◽  
Wei Li ◽  
Robert A. Copeland ◽  
Stephan N. Witt ◽  
Bih Show Lou ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Room Temperature ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

Structural characterization of nitric oxide-bound soluble Guanylate Cyclase using resonance Raman spectroscopy

2013 ◽  
Vol 17 (03) ◽  
pp. 240-246
Author(s):  
Biswajit Pal ◽  
Katsuhiro Tanaka ◽  
Shigeo Takenaka ◽  
Tajith B. Shaik ◽  
Teizo Kitagawa
Keyword(s):  
Nitric Oxide ◽  
Raman Spectroscopy ◽  
Guanylate Cyclase ◽  
Protein Interactions ◽  
Bound States ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Bending Modes

Mammalian soluble Guanylate Cyclase (sGC), working as a physiological NO receptor, is investigated using resonance Raman spectroscopy for NO bound states with different saturation levels in the presence and absence of effectors. The Fe–NO (νFe–NO) and N–O (νN-O) stretching bands appeared at 521 and 1681 cm-1, respectively, without effectors, but νN-O was split into 1681 and 1699 cm-1 in the presence of GTP and shifted to 1687 cm-1 in the presence of YC-1 or BAY 41-2272, while νFe-NO remained unaltered. The split two νN-O bands were independent of NO saturation levels. GTP or YC-1/BAY 41-2272 altered the vinyl and propionate bending modes from 423 to 399 cm-1 and 376 to 367 cm-1, respectively. Based on these observations, allosteric effects on NO …protein interactions are discussed.

Characterization of Recombinant Horseradish Peroxidase C and three Site-Directed mutants, F41V, F41W, and R38K by Resonance Raman Spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (23) ◽  
pp. 7398-7407 ◽  
Author(s):  
Giulietta Smulevich ◽  
Mauro Paoli ◽  
Julian F. Burke ◽  
Andrew T. Smith ◽  
Stephen A. Sanders ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Horseradish Peroxidase ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Recombinant Horseradish Peroxidase
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