A resonance Raman study on the reaction intermediates of D-amino acid oxidase

Journal of Biochemistry
R MiuraT Yamano


Resonance Raman (RR) spectra of two reaction intermediates of D-amino acid oxidase with substrate analogs were obtained. The reaction intermediates studied were (1) the one in the aerobic oxidative reaction of the enzyme with beta-cyano-D-alanine and (2) the other in the reverse reductive reaction of the enzyme with chloropyruvate and ammonium. Both intermediates are characterized with the charge transfer absorption bands in the long wavelength region extending beyond 600 nm. The RR spectra of the two intermediates excited at 488.0 or 514.5 nm are those of oxidized flavin, which is consistent with our previous assumption that oxidized flavin is involved in these reaction intermediates. Relatively simple RR spectra were obtained for these intermediates with excitation at 632.8 nm which is within the region of the charge transfer bands. The resonance enhancement for the Raman lines around 1585 and 1350 cm-1 for either of the intermediates with excitation in the region of the charge transfer bands suggests that the charge transfer interaction involves the N(5)-C(4a) region extending to the C(10a)-N(1)-C(2) region of the isoalloxazine nucleus. The Raman line at 1657 cm-1 for the intermediate with chloropyruvate and ammonium was ass...Continue Reading


Mar 16, 2002·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·R Miura
Oct 4, 1983·Biochimica Et Biophysica Acta·M J BeneckyT G Spiro

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3-cyanoalanine, (L)-isomer
D-Amino Acid Dehydrogenase
Plasma Protein Binding Capacity
Raman Optical Activity Spectroscopy

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