The active site structure of <i>E. coli</i> HPII catalase

Dawson, John H.; Bracete, Alma M.; Huff, Ann M.; Kadkhodayan, Saloumeh; Zeitler, Caroline M.; Sono, Masanori; Chang, C. K.; Loewen, P.C.

doi:10.1016/0014-5793(91)81401-s

Cited by 23 publications

(30 citation statements)

References 21 publications

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“…Nature employs reduced porphyrin prosthetic groups such as chlorins (1) in catalases from E. coli (HPII) (2,3) and N. crassa (4), terminal oxidases from E. coli (5), sulfite and nitrite reductases (6), and sulfmyoglobin (7). Typically green in color, such proteins have spectral properties that differ significantly from heme proteins with fully conjugated iron porphyrins.…”

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confidence: 99%

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Coulter

Cheek

Ledbetter

et al. 2000

Biochemical and Biophysical Research Communications

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confidence: 99%

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Coulter

Cheek

Ledbetter

et al. 2000

Biochemical and Biophysical Research Communications

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“…The appearance of bands at 640 nm and the weak m.c.d. signal under the Soret band at 403 nm are characteristics of high-spin ferric haems (Browett and Stillman, 1979;Eglinton et al, 1983;Dawson and Dooley, 1989 Figure 4 shows three spectra recorded over a 2 h period. As with HRP I, even in the absence of a specific electron donor, these compound I species will scavenge electrons and slowly reduce to compound II, and subsequently to the native enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…This green intermediate is the highest oxidation state available for the ferric haem group and contains two electrons less than the resting ferric haem. The chemical, biochemical and spectroscopic properties of the compound I species of both catalases and peroxidases has long been the subject of detailed studies (Dawson and Dooley, 1989). For catalase, the catalatic reaction proceeds in-two single steps, first oxidation of the ferric haem by H 02, then reduction of the haem by a-second molecule of H202 to form water and 02, according to the following scheme:…”

Section: Introductionmentioning

confidence: 99%

“…The spectral properties of these species have been studied extensively in order to interpret the role of the electronic structure of the iron and the porphyrin ring in the observed enzymatic chemistry (Strickland et al, 1968;Fajer et al, 1973;Stillman et al, 1975Dunford and Stillman, 1976;Morishima and Ogawa, 1978;Browett and Stillman, 1979, 1981aDolphin, 1981;Hanson et al, 1981;Teraoka et al, 1982;Browett et al, 1983a,b;Sievers et al, 1983;Fujita et al, 1983;Ohlsson et al, 1984;Oertling and Babcock, 1985;van Wart and Zimmer, 1985;Penner-Hahn et al, 1986;Foote et al, 1987;Oertling et al, 1987;Ogura and Kitagawa, 1987;Browett et al, 1988;Gasyna et al, 1988a;Dawson et al, 1991;Loew et al, 1991;Du et al, 1991;Du and Loew, 1992). The absorption spectra of HRP I and catalase I have long puzzled spectroscopists, as these spectra are quite unique.…”

Section: Introductionmentioning

confidence: 99%

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Analysis of the optical absorption and magnetic-circular-dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase

Marañón

Mercier

Huystee

et al. 1994

Biochemical Journal

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The electronic structures of the cationic isoenzyme of peanut peroxidase, horseradish peroxidase (isoenzyme C) and bovine liver catalase are compared through analysis of their optical absorption and magnetic c.d. (m.c.d.) spectral properties. The spectral data for the native resting states and compounds I and II of peanut peroxidase (PeP) are reported. The absorption and m.c.d. data for the native PeP exhibit bands characteristic of the high-spin ferric haem. The absorption spectrum of PeP compound I closely resembles that observed for the HRP compound I species. The m.c.d. data for PeP I clearly identifies that ring oxidation has occurred. One-electron reduction forms the PeP compound II species. The absorption and m.c.d. spectra recorded for PeP II exhibit the well-resolved spectral characteristics previously observed for both HRP compound II and catalase compound II. The spectral data of PeP with HRP and catalase are compared. The data clearly indicate that the m.c.d. spectral patterns of both plant peroxidases (PeP and HRP) are very similar and, therefore, the electronic structures of their resting states, and as well their primary and secondary compounds, must be similar. The m.c.d. data suggest that, while the compound I species of PeP and HRP belong to one electronic class, catalase compound I belongs to a different class. These data emphasize how the ground states of these two classes of oxidized haem, may be characterized as predominantly 2A2u (PeP I and HRP I) or 2A1u (catalase I). Peanut peroxidase is the second plant peroxidase for which the electronic structure of the compound I intermediate has been studied using the m.c.d. technique. The similarities with horseradish peroxidase allow us to suggest that plant peroxidases may operate by the same general mechanism, in spite of the low degree of sequence similarity between their polypeptide chains.

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“…therein), revealed the presence of novel tyrosinate (O-) ligation to the 5-coordinate ferric heme of the native enzyme. Tyrosinate is not known to be a ligand for any other native heme protein, although it has been proposed for the green chlorin (iron dihydroporphyrin) catalases from Neurospora crassa and E. coli [6,7].…”

Section: Introductionmentioning

confidence: 99%

Comparative analysis of catalases: spectral evidence against heme‐bound water for the solution enzymes

et al. 1995

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A recent X-ray structural analysis of M. luteus catalase indicates heine-bound H20 trans to the proximal tyrosinate ligand, a finding in contrast to previous X-ray data reporting a 5-coordinate heine for bovine liver catalase. The presence of heine-bound H20, requiring displacement prior to substrate-binding, is likely to be catalytically significant for catalases. We have used magnetic circular dichroism (MCD) spectroscopy, a highly accurate method for assignment of heine spin-and coordinationstates, to study native, solution forms of bovine liver, M. luteus, and A. niger catalases. All three enzymes display similar spectral features with the weak (~5 ,Ae M [moles.cm.Tesla] -1) intensity typical of a 5-coordinate high-spin ferric heine. No evidence for H20-ligation, inducing a 6-coordinate heine, occurred upon variation of pH or buffer composition. Therefore, we suggest that the catalytically significant structure of catalases has an unoccupied heme binding site trans to the proximal tyrosinate heine ligand.

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The active site structure of E. coli HPII catalase

Cited by 23 publications

References 21 publications

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Analysis of the optical absorption and magnetic-circular-dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase

Comparative analysis of catalases: spectral evidence against heme‐bound water for the solution enzymes

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