Catalase-Peroxidase from Synechocystis Is Capable of Chlorination and Bromination Reactions

Jakopitsch, Christa; Regelsberger, Günther; Furtmüller, Paul G.; Rüker, Florian; Peschek, Günter A.; Obinger, Christian

doi:10.1006/bbrc.2001.5616

Cited by 50 publications

(31 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There is a correlation between the standard reduction potential of the ferric/ferrous couple and the stability of high valent porphyrin species (25). In the case of catalase-peroxidases the standard reduction potential of the ferric/ferrous couple of M. tuberculosis KatG was determined to be Ϫ50 mV (26), which is much more positive than that of other plant-type peroxidases (27). This fits with the observation that Synechocystis KatG is able to oxidize chloride (27) a two-electron oxidation reaction, which needs a redox potential of the KatG couple compound I/native enzyme to exceed 1.1 V. But regarding the catalatic reactivity (i.e.…”

Section: Effect On the Chemical Nature Of The Radical Intermediates Imentioning

confidence: 97%

Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

Jakopitsch¹,

Ivancich

Schmuckenschlager³

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Catalase-peroxidases (KatGs) are heme peroxidases with a catalatic activity comparable to monofunctional catalases. They contain an unusual covalent distal side adduct with the side chains of Trp 122 , Tyr 249 , and Met 275 (Synechocysis KatG numbering). The known crystal structures suggest that Tyr 249 and Met 275 could be within hydrogen-bonding distance to Arg 439 . To investigate the role of this peculiar adduct, the variants Y249F, M275I, R439A, and R439N were investigated by electronic absorption, steady-state and transient-state kinetic techniques and EPR spectroscopy combined with deuterium labeling. Exchange of these conserved residues exhibited dramatic consequences on the bifunctional activity of this peroxidase. The turnover numbers of catalase activity of M275I, Y249F, R439A, and R439N are 0.6, 0.17, 4.9, and 3.14% of wild-type activity, respectively. By contrast, the peroxidase activity was unaffected or even enhanced, in particular for the M275I variant. As shown by mass spectrometry and EPR spectra, the KatG typical adduct is intact in both Arg 439 variants, as is the case of the wild-type enzyme, whereas in the M275I variant the covalent link exists only between Tyr 249 and Trp 122 . In the Y249F variant, the link is absent. EPR studies showed that the radical species formed upon reaction of the Y249F and R439A/N variants with peroxoacetic acid are the oxoferrylporphyrin radical, the tryptophanyl and the tyrosyl radicals, as in the wild-type enzyme. The dramatic loss in catalase activity of the Y249F variant allowed the comparison of the radical species formed with hydrogen peroxide and peroxoacetic acid. The EPR data strongly suggest that the sequence of intermediates formed in the absence of a one electron donor substrate, is por ⅐ ؉ 3 Trp ⅐ (or Trp ⅐ ؉ ) 3 Tyr ⅐ . The M275I variant did not form the Trp ⅐ species because of the dramatic changes on the heme distal side, most probably induced by the repositioning of the remaining Trp 122 -Tyr 249 adduct. The results are discussed with respect to the bifunctional activity of catalase-peroxidases.Catalase-peroxidases (KatGs) 1 are present in bacteria and fungi and function primarily as hydrogen peroxide scavengers (1-3). Sequence similarities indicate they are members of the class I of the superfamily of plant, fungal, and bacterial peroxidases (4). In contrast to the other members of this group, such as cytochrome c peroxidase (CcP) and ascorbate peroxidase (APX), they show a high catalase activity comparable with monofunctional catalases. Although the catalase activity is overwhelming, KatGs also show a substantial peroxidase activity with various one electron donors.There are three crystal structures of KatGs available, namely the Archaebacterium Haloarcula marismortui (5), Burkholderia pseudomallei (6), and Synechococcus PCC 7942 (PDB entry 1UB2), the latter being a cyanobacterial KatG with high homology to Synechocystis KatG. The structures show that the arrangement of the active site is similar to CcP and APX, containing the distal triad arg...

show abstract

Section: Effect On the Chemical Nature Of The Radical Intermediates Imentioning

confidence: 97%

Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

Jakopitsch¹,

Ivancich

Schmuckenschlager³

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…An additional manganese dependence has also been suggested based on studies using the related Mycobacterium smegmatis CP (9,10), although this activity may not play an essential role in INH oxidation by the M. tuberculosis CP (8,11). However, M. tuberculosis CP has been shown to display the ability to oxidize Mn 2ϩ as well as halogenated compounds using a chloroperoxidatic activity (12).…”

mentioning

confidence: 99%

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Pierattelli

Banci

Eady

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

There is an urgent need to understand the mechanism of activation of the frontline anti-tuberculosis drug isoniazid by the Mycobacterium tuberculosis catalase-peroxidase. To address this, a combination of NMR spectroscopic, biochemical, and computational methods have been used to obtain a model of the frontline anti-tuberculosis drug isoniazid bound to the active site of the class III peroxidase, horseradish peroxidase C. This information has been used in combination with the new crystal structure of the M. tuberculosis catalase-peroxidase to predict the mode of INH binding across the class I heme peroxidase family. An enzyme-catalyzed mechanism for INH activation is proposed that brings together structural, functional, and spectroscopic data from a variety of sources. Collectively, the information not only provides a molecular basis for understanding INH activation by the M. tuberculosis catalase-peroxidase but also establishes a new conceptual framework for testing hypotheses regarding the enzyme-catalyzed turnover of this compound in a number of heme peroxidases.

show abstract

“…Anti-oxidative Stress System in Cyanobacteria-In cyanobacteria, the physiological significance of catalase-peroxidase, 2-Cys Prx, and NADPH-dependent peroxidase as anti-oxidative stress system is reported (20,21,47,48). As mentioned, the gene product of sll0755 in Synechocystis sp.…”

Section: Table II Peroxidase Activity Of the Recombinant Type Ii Prxmentioning

confidence: 98%

Anti-oxidative Stress System in Cyanobacteria

Hosoya-Matsuda

Motohashi

Yoshimura

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

Catalase-Peroxidase from Synechocystis Is Capable of Chlorination and Bromination Reactions

Cited by 50 publications

References 30 publications

Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Anti-oxidative Stress System in Cyanobacteria

Contact Info

Product

Resources

About