Resonance Raman Study of the Active Site of Coprinus cinereus Peroxidase

Smulevich, Giulietta; Feis, Alessandro; Focardi, Claudia; Tams, Jeppe Wegener; Welinder, Karen G.

doi:10.1021/bi00255a024

Cited by 60 publications

(92 citation statements)

References 47 publications

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“…The m(C=C) vinyl stretching modes are enhanced via the A-term (Franck-Condon mechanism); however, these bands are also observed in Q band excitation. This is consistent with previous observations for various heme containing peroxidases-namely CcP [24], HRPC [25], and Coprinus cinereus peroxidase (CIP) [26]-despite the fact that vinyl stretching modes are not expected to be enhanced a priori with visible excitation. The complete assignment of the high-frequency region is reported in Table S1 of the ESM.…”

Section: Spectroscopy At Room Temperaturesupporting

confidence: 92%

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

et al. 2010

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The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 a-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands.

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Section: Spectroscopy At Room Temperaturesupporting

confidence: 92%

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

et al. 2010

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“…The structure at pH 4.5 presented here may represent the physiological form of the resting enzyme and is the first example of a peroxidase with a typical pentacoordinated heine iron demonstrated by crystallography. This is consistent with the resonance Raman and NMR studies done on C. einereus peroxidase which showed that at a neutral pH the ferric state is characteristic of a fivecoordinated high-spin heme [26,27]. In CcP, LiP, MnP, and ascorbate peroxidase, a water molecule occupies the 6th position of each heme [14][15][16][17].…”

Section: Coordination To the Heme Ironsupporting

confidence: 85%

Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 Å resolution crystallographic study at pH 4.5

Kunishima¹,

Amada²,

Fukuyama³

et al. 1996

FEBS Letters

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In the presence of ammonium sulfate the absorption spectra of a peroxidase from the fungus Arthromyces ramosus (ARP) showed that the low-spin component increased as the pH increased from 6.0 to 9.0, whereas in its absence ARP remained in the high-spin state in the pH range investigated. The crystal structure of ARP at pH 4.5 in the presence of ammonium sulfate at 1.8 A resolution showed that the electron density at the 6th position of the heine iron seen at pH 7.5 had disappeared and that the iron atom deviated markedly from the heme plane. These observations strongly suggest that under physiological conditions the heine of ARP is in the pentacoordinated high-spin state and that at a high pH the heine iron is able to bind ammonia, forming the low-spin state. The location of the water molecule at the distal side of the heme in peroxidases is also discussed.

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“…6, together with those of native ferrous HRPC and its imidazole complex, for 441.6 nm excitation, where the HS form is selectively resonance-enhanced. The spectrum of the native protein recorded at 441.6 nm is essentially identical to that reported previously for excitation at 457.9 nm (36) and is characteristic of a 5-c HS heme. The same experiment was also carried out with 413.1 nm excitation, where the LS form is selectively resonance enhanced (data not shown).…”

Section: Carbon Monoxide and Bha Binding To Casupporting

confidence: 80%

The Critical Role of the Proximal Calcium Ion in the Structural Properties of Horseradish Peroxidase

Howes

Feis

Raimondi³

et al. 2001

Journal of Biological Chemistry

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The extent to which the structural Ca 2؉ ions of horseradish peroxidase (HRPC) are a determinant in defining the heme pocket architecture is investigated by electronic absorption and resonance Raman spectroscopy upon removal of one Ca 2؉ ion. The Fe(III) heme states are modified upon Ca 2؉ depletion, with an uncommon quantum mechanically mixed spin state becoming the dominant species. Ca 2؉ -depleted HRPC forms complexes with benzohydroxamic acid and CO which display spectra very similar to those of native HRPC, indicating that any changes to the distal cavity structural properties upon Ca 2؉ depletion are easily reversed. Contrary to the native protein, the Ca 2؉ -depleted ferrous form displays a low-spin bis-histidyl heme state and a small proportion of high-spin heme. Furthermore, the (Fe-Im) stretching mode downshifts 27 cm ؊1 upon Ca 2؉ depletion revealing a significant structural perturbation of the proximal cavity near the histidine ligand. The specific activity of the Ca 2؉ -depleted enzyme is 50% that of the native form. The effects on enzyme activity and spectral features observed upon Ca 2؉ depletion are reversible upon reconstitution. Evaluation of the present and previous data firmly favors the proximal Ca 2؉ ion as that which is lost upon Ca 2؉ depletion and which likely plays the more critical role in regulating the heme pocket structural and catalytic properties.Peroxidases of the plant peroxidase superfamily are hemecontaining enzymes that oxidize a variety of aromatic molecules in the presence of hydrogen peroxide. They include peroxidases of plant, fungal, and prokaryotic origins that can be divided into three classes based on sequence alignment (1).Additional support for such a classification was gained as the crystal structures of representative enzymes of each class became available. Class I contains bacterial peroxidases and peroxidases from plant mitochondria and chloroplasts, for example most ascorbate peroxidases and cytochrome c peroxidase. Class II contains extracellular fungal peroxidases such as Coprinus cinereus peroxidase (a peroxidase essentially identical to Arthromyces ramosus peroxidase) and lignin-degrading peroxidases. Class III contains secretory plant peroxidases, typified by the classical horseradish peroxidase isoenzyme C (HRPC). The peroxidases of classes II and III share a number of structural elements considered to be of importance for maintaining protein stability and activity. These include calciumbinding sites proximal and distal to the heme and four disulfide bridges (1-5); the latter was in different locations in class II with respect to class III peroxidases. These features are absent in class I peroxidases. Class III peroxidases also have a loop insertion in the sequence, composed of the DЈ, FЈ, and FЉ helices, not found in the other classes. The relationship between calcium binding and enzyme inactivation has been treated primarily by studies on lignin peroxidase (LIP) (6, 7), manganese peroxidase (MNP) (8, 9), and HRPC (10, 11). Thermal (6) and alkaline (7) i...

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Resonance Raman Study of the Active Site of Coprinus cinereus Peroxidase

Cited by 60 publications

References 47 publications

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 Å resolution crystallographic study at pH 4.5

The Critical Role of the Proximal Calcium Ion in the Structural Properties of Horseradish Peroxidase

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