EXAFS and Raman evidence for histidine binding at the active site of protocatechuate 3,4-dioxygenase

Journal Article · Fri Jan 01 00:00:00 EST 1982 · J. Am. Chem. Soc.; (United States)

DOI:https://doi.org/10.1021/ja00386a057· OSTI ID:5616932

Felton, R H; Barrow, W L; May, S W; Sowell, A L; Goel, S; Bunker, G; Stern, E A

Raman spectra of both labelled and unlabelled apoprotocatechuate 3,4-dioxygenase (PCD) were collected. The Raman spectra of both labelled and unlabelled enzyme solutions were collected in the same run to minimize monochromator positioning errors and some source fluctuations. Extended x-ray absorption fine structure (EXAFS) spectra were collected in the fluorescence mode at 250 m on samples of PCD and samples of 3-chloro-4-hydroxy-benzoate (3-C1HB). Preparation of protocatechuate-3,4-dioxyenase, its /sup 34/S-labelled species, apo-PCD, and its /sup 54/Fe-labelled species is described. The spectral variations are interpreted.

• Research Organization: Georgia Institute of Technology, Atlanta
• OSTI ID: 5616932
• Journal Information: J. Am. Chem. Soc.; (United States), Vol. 104:22
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
IRON 54
CHEMICAL PREPARATION
OXYGENASES
FINE STRUCTURE
RAMAN SPECTRA
SULFUR 34
LABELLED COMPOUNDS
X-RAY SPECTRA
ENZYMES
EVEN-EVEN NUCLEI
INTERMEDIATE MASS NUCLEI
IRON ISOTOPES
ISOTOPES
LIGHT NUCLEI
NUCLEI
OXIDOREDUCTASES
SPECTRA
STABLE ISOTOPES
SULFUR ISOTOPES
SYNTHESIS
400302* - Organic Chemistry- Isotope Effects- (-1987)
400103 - Radiometric & Radiochemical Procedures- (-1987)