CaltechAUTHORS
  A Caltech Library Service

Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy

Wang, Sophie X. and Nakamura, Nobuhumi and Mure, Minae and Klinman, Judith P. and Sanders-Loehr, Joann (1997) Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy. Journal of Biological Chemistry, 272 (46). pp. 28841-28844. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:20120203-075846359

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20120203-075846359

Abstract

Lysine tyrosylquinone (LTQ) recently has been identified as the active site cofactor in lysyl oxidase by isolation and characterization of a derivatized active site peptide. Reported in this study is the first characterization of the underivatized cofactor in native lysyl oxidase by resonance Raman (RR) spectrometry. The spectrum is characterized by a unique set of vibrational modes in the 1200 to 1700 cm^(−1) region. We show that the RR spectrum of lysyl oxidase closely matches that of a synthetic LTQ model compound, 4-n-butylamino-5-ethyl-1,2-benzoquinone, in aqueous solutions but differs significantly from those of other topa quinone-containing amine oxidases under similar conditions. Furthermore, we have observed the same ^(18)O shift of the C=O stretch in both the lysyl oxidase enzyme and the LTQ cofactor model compound. The RR spectra of different model compounds and their D shifts give additional evidence for the protonation state of LTQ cofactor in the enzyme. The overall similarity of these spectra and their shifts shows that the lysyl oxidase cofactor and the model LTQ compound have the same structure and properties. These data provide strong and independent support for the new cofactor structure, unambiguously ruling out the possibility that the structure originally reported had been derived from a spurious side reaction during the derivatization of the protein and isolation of the active site peptide.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1074/jbc.272.46.28841DOIUNSPECIFIED
http://www.jbc.org/content/272/46/28841PublisherUNSPECIFIED
Additional Information:© 1997 by The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, September 3, 1997, and in revised form, September 23, 1997. This work was supported by National Institutes of Health Grants GM-39296 (to J. P. K.) and GM-34468 (to J. S.-L.), as well as support from the W. M. Keck Foundation (to J. P. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. We are grateful to Dr. David M. Dooley and Doreen E. Brown for the sample of pea seedling amine oxidase. We also want to thank Hitoshi Yamada at ISIR, Osaka University for the assistance in mass spectrometric analysis of the model compounds.
Funders:
Funding AgencyGrant Number
NIHGM-39296
NIHGM-34468
W. M. Keck FoundationUNSPECIFIED
Record Number:CaltechAUTHORS:20120203-075846359
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20120203-075846359
Official Citation: Sophie X. Wang, Nobuhumi Nakamura, Minae Mure, Judith P. Klinman, and Joann Sanders-Loehr Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy J. Biol. Chem. 1997 272: 28841-28844. doi:10.1074/jbc.272.46.28841
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:29107
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:03 Feb 2012 16:24
Last Modified:03 Feb 2012 16:24

Repository Staff Only: item control page