Direct observation of the titration of substrate carbonyl groups in the active site of .alpha.-chymotrypsin by resonance Raman spectroscopy

Biochemistry ◽  
1989 ◽  
Vol 28 (16) ◽  
pp. 6701-6709 ◽  
Author(s):  
Peter J. Tonge ◽  
Paul R. Carey
Keyword(s):  
Raman Spectroscopy ◽  
Direct Observation ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Carbonyl Groups

scholarly journals Back Cover: Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases (Angew. Chem. Int. Ed. 19/2013)

2013 ◽  
Vol 52 (19) ◽  
pp. 5186-5186
Author(s):  
Elisabeth Siebert ◽  
Marius Horch ◽  
Yvonne Rippers ◽  
Johannes Fritsch ◽  
Stefan Frielingsdorf ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Back Cover

Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases

2013 ◽  
Vol 52 (19) ◽  
pp. 5162-5165 ◽  
Author(s):  
Elisabeth Siebert ◽  
Marius Horch ◽  
Yvonne Rippers ◽  
Johannes Fritsch ◽  
Stefan Frielingsdorf ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

Vibrations of the scissile C—O bond in an acyl-chymotrypsin observed by resonance Raman spectroscopy

1983 ◽  
Vol 61 (11) ◽  
pp. 2590-2595 ◽  
Author(s):  
P. R. Carey ◽  
D. J. Phelps
Keyword(s):  
Raman Spectroscopy ◽  
Carbon Atom ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Acyl Moiety ◽  
Unsaturated Ester ◽  
Carbonyl Carbon Atom ◽  
Carbonyl Carbon ◽  
Stretching Vibration

5-Methylthienylacryloyl chymotrypsin has been prepared with 13C at the carbonyl and, separately, at the α carbon atoms of the acyl moiety. The isotopically labelled species confirm the assignments of several of the bands in the resonance Raman (RR) spectrum of the acyl-enzyme and show that the feature occurring near 1260 cm−1 involves the motion of the carbonyl carbon atom. It is likely that the 1260 cm−1 band is associated with the stretching vibration of the C—O bond in the =C—C(=O)—O— chymotrypsin moiety, i.e. the vibration of the bond being cleaved in the active site. A moderately intense 1260 cm−1 feature occurs only in the RR spectrum of the native acyl-enzyme and possible reasons are given for its appearance. The labelled species also confirm that the bands appearing near 1715 cm−1 in the RR spectrum of the acyl-enzyme are associated with the stretching mode of the acyl carbonyl, νC=O. This frequency is that expected for an unperturbed α, β-unsaturated ester. Additionally, RR data are presented for 5-methylthienylacrylic acid in its —COOH and —COO− forms labelled with 13C at the C=O and α carbon positions.

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