The crystal structure of chloroperoxidase: a heme peroxidase–cytochrome P450 functional hybrid

Sundaramoorthy, Munirathinam; Terner, James; Poulos, T.L.

doi:10.1016/s0969-2126(01)00274-x

Cited by 437 publications

(438 citation statements)

References 48 publications

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“…In DyP, Asp 171 appears to play the role fulfilled by the distal histidine in other peroxidases. A similar (but not identical) case is CPO where glutamic acid substitutes for the distal histidine (11). Notably, homology analyses of primary structures reveal that residues corresponding to His 308 , Asp 171 , and Arg 329 in DyP are conserved in cpop21 and TAP.…”

Section: Resultsmentioning

confidence: 98%

“…Similarly, CPO lacks distal histidine. Instead, histidine at this position is replaced with glutamic acid (11). However, a histidine existing near the heme distal area of CPO has been postulated to be indirectly involved in modulating the acidity/basicity of the carbonyl group of glutamic acid.…”

Section: Discussionmentioning

confidence: 99%

“…Representatives of class II include lignin peroxidase (LiP) 2 (4), manganese peroxidase (MnP) (5), and versatile peroxidase (6,7), whereas class III contains horseradish peroxidase (HRP) (8) and barley grain peroxidase (BGP) (9). This classification has been widely applied to most known peroxidases, with the exception of chloroperoxidase (CPO) isolated from the fungus, Caldariomyces fumago, which lacks primary structural homology with other peroxidases (10,11). However, in contrast to the plant peroxidases, those from animals, including mammals, are yet to be categorized.…”

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confidence: 99%

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DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

Sugano

Muramatsu

Ichiyanagi

et al. 2007

Journal of Biological Chemistry

199

285

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DyP, a unique dye-decolorizing enzyme from the fungus Thanatephorus cucumeris Dec 1, has been classified as a peroxidase but lacks homology to almost all other known plant peroxidases. The primary structure of DyP shows moderate sequence homology to only two known proteins: the peroxidedependent phenol oxidase, TAP, and the hypothetical peroxidase, cpop21. Here, we show the first crystal structure of DyP and reveal that this protein has a unique tertiary structure with a distal heme region that differs from that of most other peroxidases. DyP lacks an important histidine residue known to assist in the formation of a Fe 4؉ oxoferryl center and a porphyrinbased cation radical intermediate (compound I) during the action of ubiquitous peroxidases. Instead, our tertiary structural and spectrophotometric analyses of DyP suggest that an aspartic acid and an arginine are involved in the formation of compound I. Sequence analysis reveals that the important aspartic acid and arginine mentioned above and histidine of the heme ligand are conserved among DyP, TAP, and cpop21, and structural and phylogenetic analyses confirmed that these three enzymes do not belong to any other families of peroxidase. These findings, which strongly suggest that DyP is a representative heme peroxidase from a novel family, should facilitate the identification of additional new family members and accelerate the classification of this novel peroxidase family.Peroxidases have been systematically researched for more than 70 years. Fifteen years ago, Welinder (1) proposed the concept of a "plant peroxidase superfamily" comprising classes I, II, and III, based on primary sequence alignments and isolation from prokaryotes, fungi, and plants, respectively. Using this strategy, yeast cytochrome c peroxidase (2) and chloroplast ascorbate peroxidase (3) were classified as class I peroxidases on account of their prokaryotic source. Representatives of class II include lignin peroxidase (LiP) 2 (4), manganese peroxidase (MnP) (5), and versatile peroxidase (6, 7), whereas class III contains horseradish peroxidase (HRP) (8) and barley grain peroxidase (BGP) (9). This classification has been widely applied to most known peroxidases, with the exception of chloroperoxidase (CPO) isolated from the fungus, Caldariomyces fumago, which lacks primary structural homology with other peroxidases (10, 11). However, in contrast to the plant peroxidases, those from animals, including mammals, are yet to be categorized. To date, most of these enzymes have been grouped into the plant or animal peroxidase superfamily (12).So far, we isolated and characterized a novel extracellular peroxidase, DyP, from the fungus Thanatephorus cucumeris Dec 1 (13-16). DyP, a glycoprotein having one heme as a cofactor, has a molecular mass of 58 kDa and requires H 2 O 2 for all enzyme reactions, indicating that it functions as a peroxidase. DyP has several characteristics that distinguish it from all other peroxidases, including a particularly wide substrate specificity, a lack of homology to m...

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Section: Resultsmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

Sugano

Muramatsu

Ichiyanagi

et al. 2007

Journal of Biological Chemistry

199

285

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“…In highly weathered leaves from the forest floor, insoluble aromatic Cl org hotspots are common and often coincide with elevated Fe. Metals such as Fe are often the key cofactors in the reaction centers of haloperoxidative enzymes (Sundaramoorthy et al, 1995). In addition, abiotic (non-enzymatic) metal-catalyzed chlorination of aliphatic and aromatic substrates has been documented in natural systems (Keppler et al, 2000;Schoeler and Keppler, 2002;Fahimi et al, 2003;Holmstrand et al, 2006) and as part of biomimetic synthetic schemes in the laboratory (Delaude and Laszlo, 1990;Walker et al, 1997).…”

Section: Summary and Implications For The Formation Of Different CL Omentioning

confidence: 99%

X-ray spectromicroscopic investigation of natural organochlorine distribution in weathering plant material

Leri

Marcus

Myneni

2007

Geochimica et Cosmochimica Acta

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“…cytochromes a, b, c and f) [1][2][3] which cycle between low-spin Fe(II) and low-spin Fe(III), small molecule binding and transport, 4,5 catalysis and O 2 activation (e.g. peroxidases and cytochromes P450) [6][7][8][9][10][11] where high valent Fe centers are involved in H atom abstraction, hydroxylation and epoxide formation. Heme sites are fundamentally different from non-heme iron sites in that the porphyrin ligand allows for the delocalization of the iron d electrons into the porphyrin π system.…”

Section: Introductionmentioning

confidence: 99%

Fe L-Edge X-ray Absorption Spectroscopy of Low-Spin Heme Relative to Non-heme Fe Complexes: Delocalization of Fe d-Electrons into the Porphyrin Ligand

et al. 2006

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Hemes (iron porphyrins) are involved in a range of functions in biology including electron transfer, small molecule binding and transport, and O 2 activation. The delocalization of the Fe d-electrons into the porphyrin ring and its effect on the redox chemistry and reactivity of these systems has been difficult to study by optical spectroscopies due to the dominant porphyrin π → π* transitions which obscure the metal center. Recently we have developed a methodology that allows for the interpretation of the multiplet structure of Fe L-edges in terms of differential orbital covalency (i.e. differences in mixing of the d-orbitals with ligand orbitals) using a valence bond configuration interaction (VBCI) model. Applied to low spin heme systems, this methodology allows experimental determination of the delocalization of the Fe d-electrons into the porphyrin (p) ring both in terms of P→Fe σ and π donation and Fe→P π back-bonding. We find that π donation to Fe(III) is much larger than π back-bonding from Fe(II), indicating that a hole super-exchange pathway dominates electron transfer. The implications of the results are also discussed in terms of the differences between heme and non-heme oxygen activation chemistry.

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The crystal structure of chloroperoxidase: a heme peroxidase–cytochrome P450 functional hybrid

Cited by 437 publications

References 48 publications

DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

X-ray spectromicroscopic investigation of natural organochlorine distribution in weathering plant material

Fe L-Edge X-ray Absorption Spectroscopy of Low-Spin Heme Relative to Non-heme Fe Complexes: Delocalization of Fe d-Electrons into the Porphyrin Ligand

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