Distinct heme active-site structure in lactoperoxidase revealed by resonance Raman spectroscopy

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10125-10130 ◽  
Author(s):  
Songzhou Hu ◽  
Robert W. Treat ◽  
James R. Kincaid
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Site Structure ◽  
Active Site Structure

The active site structure ofba3 oxidase fromThermus thermophilus studied by resonance Raman spectroscopy

1999 ◽  
Vol 5 (S5) ◽  
pp. S53-S63 ◽  
Author(s):  
S. Gerscher ◽  
P. Hildebrandt ◽  
G. Buse ◽  
T. Soulimane
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Site Structure ◽  
Active Site Structure

Resonance Raman Spectroscopy and Quantum Chemical Calculations Reveal Structural Changes in the Active Site of Photoactive Yellow Protein†

Biochemistry ◽  
2002 ◽  
Vol 41 (17) ◽  
pp. 5668-5674 ◽  
Author(s):  
Masashi Unno ◽  
Masato Kumauchi ◽  
Jun Sasaki ◽  
Fumio Tokunaga ◽  
Seigo Yamauchi
Keyword(s):  
Raman Spectroscopy ◽  
Quantum Chemical Calculations ◽  
Active Site ◽  
Quantum Chemical ◽  
Structural Changes ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Photoactive Yellow Protein

Hemocyanin Active Site Characterization by EXAFS and Resonance Raman Spectroscopy

1982 ◽  
pp. 291-304
Author(s):  
T.G. Spiro ◽  
J.M. Brown ◽  
J.A. Larrabee ◽  
L. Powers ◽  
B. Kincaid
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Site Characterization

Ultraviolet Resonance Raman Spectroscopy of .DELTA.5-3-Ketosteroid Isomerase Revisited: Substrate Polarization by Active-Site Residues

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4441-4447 ◽  
Author(s):  
Janina C. Austin ◽  
Qinjian Zhao ◽  
Trace Jordan ◽  
Paul Talalay ◽  
Albert S. Mildvan ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Active Site Residues ◽  
Ketosteroid Isomerase ◽  
Ultraviolet Resonance Raman Spectroscopy ◽  
Ultraviolet Resonance Raman

Characterization of the siroheme active site in spinach nitrite reductase by resonance Raman spectroscopy

1985 ◽  
Vol 830 (2) ◽  
pp. 159-163 ◽  
Author(s):  
Mark R. Ondrias ◽  
Susan D. Carson ◽  
Masakazu Hirasawa ◽  
David B. Knaff
Keyword(s):  
Raman Spectroscopy ◽  
Nitrite Reductase ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

1991 ◽  
Author(s):  
Paul R. Carey ◽  
Munsok Kim ◽  
Peter J. Tonge
Keyword(s):  
Raman Spectroscopy ◽  
Time Resolution ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

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

The Active Site Structure of Hemea33+C⋮NCuB2+of Cytochromeaa3Oxidase as Revealed from Resonance Raman Scattering

2003 ◽  
Vol 107 (36) ◽  
pp. 9865-9868 ◽  
Author(s):  
Eftychia Pinakoulaki ◽  
Magdalini Vamvouka ◽  
Constantinos Varotsis
Keyword(s):  
Raman Scattering ◽  
Active Site ◽  
Resonance Raman ◽  
Resonance Raman Scattering ◽  
Site Structure ◽  
Active Site Structure

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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