Resonance Raman studies of pyrocatechase-inhibitor complexes
- 10 June 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (12), 2588-2593
- https://doi.org/10.1021/bi00553a009
Abstract
The resonance Raman spectra of [Pseudomonas arvilla] native pyrocatechase and its benzoate and phenolate complexes were investigated by using the available lines of an argon and a krypton laser. The data provide evidence for the presence of 2 distinct tyrosines coordinated to the active-site iron. The 2 tyrosines exhibit different .nu.CO values which show maximum resonance enhancements at different excitation wavelengths. One tyrosine is more susceptible to changes in the active-site environment. Pyrocatechase is the only example among Fe-tyrosinate proteins where the tyrosines coordinating the Fe are distinguishable.This publication has 14 references indexed in Scilit:
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