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 Manthey, J. A. Articles by Chan, S. I. Search for Related Content PubMed PubMed Citation Articles by Manthey, J. A. Articles by Chan, S. I. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 15, 6734-6741, 05, 1986

Resonance Raman studies of lactoperoxidase

JA Manthey, NJ Boldt, DF Bocian and SI Chan

Resonance Raman (RR) spectra obtained at three excitation wavelengths are reported for various ferric, ferrous, and ferryl derivatives of bovine lactoperoxidase. The RR spectra of the ferric derivatives show the full complement of the vinyl stretching and scissor modes indicating that the two vinyls in the protoporphyrin IX prosthetic group are present in unmodified forms. The cysteine thiol complex exhibits a RR spectrum identical to that of the native enzyme, an observation which strongly suggests a nonheme binding site for the thiol substrates. The different ferrous complexes of lactoperoxidase which result from heme reduction at slightly alkaline and acidic pH gave identical low-frequency RR spectra. Differences are observed, however, in the high-frequency region. Reduction in the presence of cyanide, however, yields two time-resolved complexes. Changes in the ligand field during the conversion to the final form of the cyanoferrous complex are proposed based on the changes observed in the low-frequency vibrational spectrum. Comparisons are made between the low-frequency RR spectra of the limiting form of the cyanoferrous and the nitric oxide lactoperoxidase complexes. The similarity between the RR spectra of these two complexes in the 150-500 cm-1 region supports the assignment of structures for these complexes where the six- coordinate heme iron is displaced from the heme plane and away from the proximal histidine ligand.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. Galijasevic, G. M. Saed, M. P. Diamond, and H. M. Abu-Soud High Dissociation Rate Constant of Ferrous-Dioxy Complex Linked to the Catalase-like Activity in Lactoperoxidase J. Biol. Chem., September 17, 2004; 279(38): 39465 - 39470. [Abstract] [Full Text] [PDF]

				C. Ciaccio, G. De Sanctis, S. Marini, F. Sinibaldi, R. Santucci, A. Arcovito, A. Bellelli, E. Ghibaudi, P. Ferrari Rosa, and M. Coletta Proton Linkage for CO Binding and Redox Properties of Bovine Lactoperoxidase Biophys. J., January 1, 2004; 86(1): 448 - 454. [Abstract] [Full Text] [PDF]

				L. A. Andersson, S. A. Bylkas, and A. E. Wilson Spectral Analysis of Lactoperoxidase J. Biol. Chem., February 16, 1996; 271(7): 3406 - 3412. [Abstract] [Full Text] [PDF]

				H. M. Abu-Soud and S. L. Hazen Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases J. Biol. Chem., November 22, 2000; 275(48): 37524 - 37532. [Abstract] [Full Text] [PDF]