Nanosecond emission anisotropy of interacting enzymes aspartate aminotransferase glutamate dehydrogenase

Jorge E. Churchich*, Yan-Hwa Wu Lee

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Nanosecond fluorescence studies were performed on mitochondrial aspartate aminotransferase from beef liver to determine whether the dimeric enzyme displays any modes of flexibility in the nanosecond range. The most informative quantities calculated from nanosecond fluorescence measurements S(t) and D(t) decay in a monoexponential manner with decay times τS=13 and τD=10 nanoseconds respectively. The observed rotational correlation time θ=43 M-seconds yields a volume for the dimeric enzyme of 1.97 × 105 Ao3. The rotational correlation time of aspartate aminotransferase is influenced by the presence of the enzyme glutamate dehydrogenase.

Original languageEnglish
Pages (from-to)409-416
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume68
Issue number2
DOIs
StatePublished - 26 Jan 1976

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