Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 18 August 1989:
Vol. 245. no. 4919, pp. 738 - 740
DOI: 10.1126/science.2549632
Prev | Table of Contents | Next

Articles

Science, Vol 245, Issue 4919, 738-740
Copyright © 1989 by American Association for the Advancement of Science

articles

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES

M Sivaraja, DB Goodin, M Smith, and BM Hoffman

Department of Chemistry, Northwestern University, Evanston, IL 60208.

The chemical identity of the amino acid free-radical site that represents one of the two oxidizing equivalents stored in the H2O2-oxidized intermediate (compound ES) of the mitochondrial heme enzyme, cytochrome c peroxidase (CcP) has been sought for almost a quarter of a century. Site-directed mutagenesis alone cannot yield this answer. Low-temperature 35-gigahertz (Q-band) electron nuclear double resonance (ENDOR) spectroscopy was used to examine compound ES prepared from proteins containing specifically deuterated methionine or tryptophan, as well as the amino acid replacement Trp51----Phe. The results definitely identify the site of the radical in compound ES as tryptophan, most likely Trp191.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.
A. T. Smith, W. A. Doyle, P. Dorlet, and A. Ivancich (2009)
PNAS 106, 16084-16089
   Abstract »    Full Text »    PDF »
Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton.
M. Makino, H. Sugimoto, Y. Shiro, S. Asamizu, H. Onaka, and S. Nagano (2007)
PNAS 104, 11591-11596
   Abstract »    Full Text »    PDF »
Prostaglandin Endoperoxide H Synthases: PEROXIDASE HYDROPEROXIDE SPECIFICITY AND CYCLOOXYGENASE ACTIVATION.
J. Liu, S. A. Seibold, C. J. Rieke, I. Song, R. I. Cukier, and W. L. Smith (2007)
J. Biol. Chem. 282, 18233-18244
   Abstract »    Full Text »    PDF »
Reaction of Mycobacterium tuberculosis Truncated Hemoglobin O with Hydrogen Peroxide: EVIDENCE FOR PEROXIDATIC ACTIVITY AND FORMATION OF PROTEIN-BASED RADICALS.
H. Ouellet, K. Ranguelova, M. LaBarre, J. B. Wittenberg, B. A. Wittenberg, R. S. Magliozzo, and M. Guertin (2007)
J. Biol. Chem. 282, 7491-7503
   Abstract »    Full Text »    PDF »
A Tryptophan Neutral Radical in the Oxidized State of Versatile Peroxidase from Pleurotus eryngii: A COMBINED MULTIFREQUENCY EPR AND DENSITY FUNCTIONAL THEORY STUDY.
R. Pogni, M. C. Baratto, C. Teutloff, S. Giansanti, F. J. Ruiz-Duenas, T. Choinowski, K. Piontek, A. T. Martinez, F. Lendzian, and R. Basosi (2006)
J. Biol. Chem. 281, 9517-9526
   Abstract »    Full Text »    PDF »
Reaction of Ferric Cytochrome P450cam with Peracids: KINETIC CHARACTERIZATION OF INTERMEDIATES ON THE REACTION PATHWAY.
T. Spolitak, J. H. Dawson, and D. P. Ballou (2005)
J. Biol. Chem. 280, 20300-20309
   Abstract »    Full Text »    PDF »
Kinetics of Interconversion of Ferrous Enzymes, Compound II and Compound III, of Wild-type Synechocystis Catalase-peroxidase and Y249F: PROPOSAL FOR THE CATALATIC MECHANISM.
C. Jakopitsch, A. Wanasinghe, W. Jantschko, P. G. Furtmuller, and C. Obinger (2005)
J. Biol. Chem. 280, 9037-9042
   Abstract »    Full Text »    PDF »
Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase: A STOPPED-FLOW AND EPR CHARACTERIZATION OF THE MET275, TYR249, AND ARG439 VARIANTS.
C. Jakopitsch, A. Ivancich, F. Schmuckenschlager, A. Wanasinghe, G. Poltl, P. G. Furtmuller, F. Ruker, and C. Obinger (2004)
J. Biol. Chem. 279, 46082-46095
   Abstract »    Full Text »    PDF »
Crystal Structure of Mycobacterium tuberculosis Catalase-Peroxidase.
T. Bertrand, N. A. J. Eady, J. N. Jones, Jesmin, J. M. Nagy, B. Jamart-Gregoire, E. L. Raven, and K. A. Brown (2004)
J. Biol. Chem. 279, 38991-38999
   Abstract »    Full Text »    PDF »
Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link.
M. Guo, B. Bhaskar, H. Li, T. P. Barrows, and T. L. Poulos (2004)
PNAS 101, 5940-5945
   Abstract »    Full Text »    PDF »
Intra- and Intermolecular Transfers of Protein Radicals in the Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide.
O. M. Lardinois and P. R. O. de Montellano (2003)
J. Biol. Chem. 278, 36214-36226
   Abstract »    Full Text »    PDF »
Total Conversion of Bifunctional Catalase-Peroxidase (KatG) to Monofunctional Peroxidase by Exchange of a Conserved Distal Side Tyrosine.
C. Jakopitsch, M. Auer, A. Ivancich, F. Ruker, P. G. Furtmuller, and C. Obinger (2003)
J. Biol. Chem. 278, 20185-20191
   Abstract »    Full Text »    PDF »
Reactions of the Class II Peroxidases, Lignin Peroxidase and Arthromyces ramosus Peroxidase, with Hydrogen Peroxide. CATALASE-LIKE ACTIVITY, COMPOUND III FORMATION, AND ENZYME INACTIVATION.
A. N. P. Hiner, J. H. Ruiz, J. N. R. Lopez, F. G. Canovas, N. C. Brisset, A. T. Smith, M. B. Arnao, and M. Acosta (2002)
J. Biol. Chem. 277, 26879-26885
   Abstract »    Full Text »    PDF »
Unusual Oxidative Chemistry of Nomega -Hydroxyarginine and N-Hydroxyguanidine Catalyzed at an Engineered Cavity in a Heme Peroxidase.
J. Hirst and D. B. Goodin (2000)
J. Biol. Chem. 275, 8582-8591
   Abstract »    Full Text »    PDF »
Conversion of an Engineered Potassium-binding Site into a Calcium-selective Site in Cytochrome c Peroxidase.
C. A. Bonagura, B. Bhaskar, M. Sundaramoorthy, and T. L. Poulos (1999)
J. Biol. Chem. 274, 37827-37833
   Abstract »    Full Text »    PDF »
A Protein Radical and Ferryl Intermediates Are Generated by Linoleate Diol Synthase, a Ferric Hemeprotein with Dioxygenase and Hydroperoxide Isomerase Activities.
C. Su, M. Sahlin, and E. H. Oliw (1998)
J. Biol. Chem. 273, 20744-20751
   Abstract »    Full Text »    PDF »
Detection of a Tryptophan Radical as an Intermediate Species in the Reaction of Horseradish Peroxidase Mutant (Phe-221 right-arrow Trp) and Hydrogen Peroxide.
A. Morimoto, M. Tanaka, S. Takahashi, K. Ishimori, H. Hori, and I. Morishima (1998)
J. Biol. Chem. 273, 14753-14760
   Abstract »    Full Text »    PDF »
Kinetics of Transient Radicals in Escherichia coli Ribonucleotide Reductase. FORMATION OF A NEW TYROSYL RADICAL IN MUTANT PROTEIN R2.
B. Katterle, M. Sahlin, P. P. Schmidt, S. Potsch, D. T. Logan, A. Graslund, and B.-M. Sjoberg (1997)
J. Biol. Chem. 272, 10414-10421
   Abstract »    Full Text »    PDF »
Horseradish Peroxidase His-42 [IMAGE] Ala, His-42 [IMAGE] Val, and Phe-41 [IMAGE] Ala Mutants.
S. L. Newmyer and P. R. O. de Montellano (1995)
J. Biol. Chem. 270, 19430-19438
   Abstract »    Full Text »    PDF »
Horseradish Peroxidase Phe[IMAGE] [IMAGE] Tyr Mutant.
V. P. Miller, D. B. Goodin, A. E. Friedman, C. Hartmann, and P. R. O. de Montellano (1995)
J. Biol. Chem. 270, 18413-18419
   Abstract »    Full Text »    PDF »
Transient Free Radicals in Iron/Oxygen Reconstitution of Mutant Protein R2 Y122F.
M. Sahlin, Gün. Lassmann, S. Pötsch, B.-M. Sjöberg, and A. Gräslund (1995)
J. Biol. Chem. 270, 12361-12372
   Abstract »    Full Text »    PDF »
Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.
H Pelletier and J Kraut (1992)
Science 258, 1748-1755
   Abstract »    PDF »
Reaction of Human Myoglobin and H2O2. INVOLVEMENT OF A THIYL RADICAL PRODUCED AT CYSTEINE 110.
P. K. Witting, D. J. Douglas, and A. G. Mauk (2000)
J. Biol. Chem. 275, 20391-20398
   Abstract »    Full Text »    PDF »
Effect of Distal Cavity Mutations on the Formation of Compound I in Catalase-Peroxidases.
G. Regelsberger, C. Jakopitsch, F. Ruker, D. Krois, G. A. Peschek, and C. Obinger (2000)
J. Biol. Chem. 275, 22854-22861
   Abstract »    Full Text »    PDF »
Reaction of Human Myoglobin and H2O2. ELECTRON TRANSFER BETWEEN TYROSINE 103 PHENOXYL RADICAL AND CYSTEINE 110 YIELDS A PROTEIN-THIYL RADICAL.
P. K. Witting and A. G. Mauk (2001)
J. Biol. Chem. 276, 16540-16547
   Abstract »    Full Text »    PDF »
H2O2-mediated Cross-linking between Lactoperoxidase and Myoglobin. ELUCIDATION OF PROTEIN-PROTEIN RADICAL TRANSFER REACTIONS.
O. M. Lardinois and P. R. O. de Montellano (2001)
J. Biol. Chem. 276, 23186-23191
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)