HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Somers, C. E. Articles by Shapiro, B. M. Search for Related Content PubMed PubMed Citation Articles by Somers, C. E. Articles by Shapiro, B. M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 264, Issue 29, 17231-17235, Oct, 1989

The heme environment of ovoperoxidase as determined by optical spectroscopy

CE Somers and BM Shapiro
Department of Biochemistry, University of Washington, Seattle 98195.

Native ovoperoxidase exhibited an optical absorption spectrum with certain similarities to lactoperoxidase, but not horseradish peroxidase, over the pH range 4.5-11.5. Ovoperoxidase had three distinct spectral forms dependent on pH, with transitions at apparent pKa values of 6.6 and 3.0. Complexes of ovoperoxidase with CN-, N3-, F- , or when reduced and ligated to carbon monoxide, CN-, or pyridine, were distinct from other peroxidases. Ovoperoxidase formed two specific and different spectral derivatives at pH 6.0 and 8.0, either in the native state, or when combined with CN-, when reduced, or when reduced and ligated to CN-. The position of the Soret band when mixed with near- stoichiometric amounts of H2O2. This cycling was inhibited by phenylhydrazine, 3-amino-1,2,4-triazole, or low pH (less than or equal to 6). Compound II was formed when ovoperoxidase was mixed with ethyl hydrogen peroxide in a 1:3 ratio, but not with H2O2. With a great excess of H2O2, Compound III was formed at pH 8.0; at pH 6.0 or below, the Soret band shifted slightly with excess of H2O2, but Compound III was never formed. Even when ovoperoxidase was bound to proteoliaisin (Weidman, P. J., and Shapiro, B. M. (1987) J. Cell Biol. 105, 561-567), ovoperoxidase exhibited spectral characteristics of the free enzyme.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. L. Wong and G. M. Wessel Free-radical crosslinking of specific proteins alters the function of the egg extracellular matrix at fertilization Development, February 1, 2008; 135(3): 431 - 440. [Abstract] [Full Text] [PDF]

				J. L. Wong and G. M. Wessel Rendezvin: An Essential Gene Encoding Independent, Differentially Secreted Egg Proteins That Organize the Fertilization Envelope Proteome after Self-Association Mol. Biol. Cell, December 1, 2006; 17(12): 5241 - 5252. [Abstract] [Full Text] [PDF]

				W. Liu, C. E. Rogge, B. Bambai, G. Palmer, A.-L. Tsai, and R. J. Kulmacz Characterization of the Heme Environment in Arabidopsis thaliana Fatty Acid {alpha}-Dioxygenase-1 J. Biol. Chem., July 9, 2004; 279(28): 29805 - 29815. [Abstract] [Full Text] [PDF]