JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M011707200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16540-16547, May 11, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/19/16540    most recent
M011707200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Witting, P. K.
Right arrow Articles by Mauk, A. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Witting, P. K.
Right arrow Articles by Mauk, A. G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Reaction of Human Myoglobin and H2O2
ELECTRON TRANSFER BETWEEN TYROSINE 103 PHENOXYL RADICAL AND CYSTEINE 110 YIELDS A PROTEIN-THIYL RADICAL*

Paul K. Witting and A. Grant MaukDagger

From the Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada

The sequence of human myoglobin (Mb) is similar to that of other species except for a unique cysteine at position 110 (Cys110). Adding hydrogen peroxide (H2O2) to human Mb affords Trp14-peroxyl, Tyr103-phenoxyl, and Cys110-thiyl radicals and coupling of Cys110-thiyl radicals yields a homodimer through intermolecular disulfide bond formation (Witting, P. K., Douglas, D. J., and Mauk, A. G. (2000) J. Biol. Chem. 275, 20391-20398). Treating a solution of wild type Mb and H2O2 with 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) at DMPO:protein <=  10 mol/mol yields DMPO-Cys110 adducts as determined by EPR. At DMPO:protein ratios (25-50 mol/mol), both DMPO-Tyr103 and DMPO-Cys110 adducts were detected, whereas at DMPO:protein >=  100 mol/mol only DMPO-Tyr103 radicals were present. The DMPO-dependent decrease in DMPO-Cys110 was matched by a near 1:1 stoichiometric increase in DMPO-Tyr103. In contrast, reaction of the Y103F human Mb with H2O2 gave no DMPO-Cys110 at DMPO:protein <=  10 mol/mol, and only trace DMPO-Cys110 at DMPO:protein >=  100 mol/mol (i.e. conditions that consistently gave DMPO-Tyr103 in the case of wild type Mb). No detectable homodimer was formed by incubation of the Y103F variant with H2O2. However, the homodimer was detected in a mixture of both the Y103F and C110A variants of human Mb upon treatment with H2O2 (C110A:Y103F:H2O2 2:1:5 mol/mol/mol); the yield of this homodimer increased with increasing ratios of C110A:Y103F. Together, these data suggest that addition of H2O2 to human Mb can produce Cys110-thiyl radicals through an intermolecular electron transfer reaction from Cys110 to a Tyr103-phenoxyl radical.

* This work was supported by Grant O 98S 0008 from the National Heart Foundation of Australia (to P. K. W.) and Medical Research Council of Canada Grant MT-7182 (to A. G. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence be addressed: Dept. of Biochemistry and Molecular Biology, 2146 Health Sciences Mall, University of British Columbia, Vancouver, V6T 1Z3, Canada.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. Liu, S. A. Seibold, C. J. Rieke, I. Song, R. I. Cukier, and W. L. Smith
Prostaglandin Endoperoxide H Synthases: PEROXIDASE HYDROPEROXIDE SPECIFICITY AND CYCLOOXYGENASE ACTIVATION
J. Biol. Chem., June 22, 2007; 282(25): 18233 - 18244.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Q. Guo, C. D. Detweiler, and R. P. Mason
Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione: IMMUNOCHEMICAL DETECTION OF A LACTOPEROXIDASE RADICAL-DERIVED 5,5-DIMETHYL-1-PYRROLINE N-OXIDE NITRONE ADDUCT
J. Biol. Chem., March 26, 2004; 279(13): 13272 - 13283.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. J. Deterding, D. C. Ramirez, J. R. Dubin, R. P. Mason, and K. B. Tomer
Identification of Free Radicals on Hemoglobin from its Self-peroxidation Using Mass Spectrometry and Immuno-spin Trapping: OBSERVATION OF A HISTIDINYL RADICAL
J. Biol. Chem., March 19, 2004; 279(12): 11600 - 11607.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Romero, R. Radi, E. Linares, O. Augusto, C. D. Detweiler, R. P. Mason, and A. Denicola
Reaction of Human Hemoglobin with Peroxynitrite: ISOMERIZATION TO NITRATE AND SECONDARY FORMATION OF PROTEIN RADICALS
J. Biol. Chem., November 7, 2003; 278(45): 44049 - 44057.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. Milani, P.-Y. Savard, H. Ouellet, P. Ascenzi, M. Guertin, and M. Bolognesi
A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
PNAS, May 13, 2003; 100(10): 5766 - 5771.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.