PMID: 11341923May 9, 2001Paper

Electrospray ionization mass spectrometry, circular dichroism and SAXS studies of the (S)-hydroxynitrile lyase from Hevea brasiliensis

Biochimica Et Biophysica Acta
U HanefeldC Kratky

Abstract

We report on experiments pertaining to solution properties of the (S)-hydroxynitrile lyase from Hevea brasiliensis (HbHNL). Small angle X-ray scattering unequivocally established the enzyme to occur in solution as a dimer, presumably of the same structure as in the crystal. The acid induced, irreversible deactivation of HbHNL was examined by electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD) and by measuring the enzyme activity. The deactivation is paralleled by an unfolding of the enzyme. ESI-MS of this 30000 Da per monomer heavy protein demonstrated that unfolding took place in several stages which are paralleled by a decrease in enzyme activity. Unfolding can also be observed by CD spectroscopy, and there is a clear correlation between enzyme activity and unfolding as detected by ESI-MS and CD.

References

Oct 12, 1996·Annals of the New York Academy of Sciences·M HasslacherH Schwab
Nov 5, 1999·Protein Science : a Publication of the Protein Society·J ZueggC Kratky

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Citations

Jun 8, 2001·Journal of Mass Spectrometry : JMS
Nov 14, 2001·Phytochemical Analysis : PCA
Jun 6, 2008·The Journal of Biological Chemistry·Andrea SchmidtVictor S Lamzin
Mar 23, 2011·Chemical Reviews·Margarita BrovettoGustavo A Seoane

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