Raman spectrum of protocatechuate dioxygenase from Pseudomonas putida. New low frequency bands. |
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Authors: | C Bull D P Ballou I Salmeen |
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Affiliation: | Department of Biological Chemistry The University of Michigan Ann Arbor, Michigan 48109 USA;Research Staff The Ford Motor Company Dearborn, Michigan 48121 USA |
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Abstract: | The Raman spectrum (441.6 nm excitation) of protocatechuate 3,4-dioxygenase (PCD) from Pseudomonas putida shows resonance enhanced bands at 1605, 1504, 1270, 858, and 830 cm?1 which are due to the p-hydroxyphenyl group of tyrosine coordinated to iron. In addition, we observe strong resonance enhanced bands at 592 and 524 cm?1 and weak (presumably iron-ligand) vibrations at 465, 423, and 371 cm?1. Recent publications of the Raman spectrum of PCD from Pseudomonas aeruginosa (Tatsuno , J. Am. Chem. Soc. 100, 4614–4615 (1978) and Keyes , Biochem. Biophys. Res. Comm. 83, 941–945 (1978) using 488 and 514 nm excitation did not report these bands. Our 441.6 nm excitation Raman spectrum of human serum transferrin, another metalloprotein with an iron-tyrosine linkage, does not show the 592 and 524 cm?1 bands and has only two very weak bands at about 423 and 364 cm?1. We discuss several interpretations of these data. |
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