Resonance Raman spectra of bovine liver catalase: Enhancement of proximal tyrosinate vibrations

Chuang, Woei Jer; Johnson, Steve R.; Wart, Harold E. Van

doi:10.1016/0162-0134(88)85030-x

Cited by 23 publications

(23 citation statements)

References 40 publications

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“…Contrary to WT cAOS, the frequencies of the porphyrin marker lines indicate that the heme in BLC adopts a 5c/HS structure (Fig. 6, trace d), which is consistent with the reported result (33). The previous spectroscopic and x-ray crystallographic studies on cAOS suggested that the coordination structure of ferric cAOS is almost the same as that of catalase (11,12).…”

Section: Resultssupporting

confidence: 90%

On the Relationship of Coral Allene Oxide Synthase to Catalase

Tosha

Uchida

Brash

et al. 2006

Journal of Biological Chemistry

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A heme domain of coral allene oxide synthase (cAOS) catalyzes the formation of allene oxide from fatty acid hydroperoxide. Although cAOS has a similar heme active site to that of catalase, cAOS is completely lacking in catalase activity. A close look at the hydrogen-bonding possibilities around the distal His in cAOS suggested that the imidazole ring is rotated by 180°relative to that of catalase because of the hydrogen bond between Thr-66 and the distal His-67. This could contribute to the functional differences between cAOS and catalase, and to examine this possibility, we mutated Thr-66 in cAOS to Val, the corresponding residue in catalase. In contrast to the complete absence of catalase activity in wild type (WT) cAOS, T66V had a modest catalase activity. On the other hand, the mutation suppressed the native enzymatic activity of the formation of allene oxide to 14% of that of WT cAOS. In the resonance Raman spectrum, whereas WT cAOS has only a 6-coordinate/high spin heme, T66V has a 5-coordinate/high spin heme as a minor species. Because catalase adopts a 5-coordinate/high spin structure, probably the 5-coordinate/high spin portion of T66V showed the catalase activity. Furthermore, in accord with the fact that the CN affinity of catalase is higher than that of WT cAOS, the CN affinity of T66V was 8-fold higher than that of WT cAOS, indicating that the mutation could mimic the heme active site in catalase. We, therefore, propose that the hydrogen bond between Thr-66 and distal His-67 could modulate the orientation of distal His, thereby regulating the enzymatic activity in cAOS.Allene oxides formed by the enzymatic dehydration of fatty acid hydroperoxides, the lipoxygenase (LOX) 4 products of polyunsaturated fatty acids, are involved in biosynthetic pathways of plants and invertebrates. The main plant pathway leads to jasmonic acid, which seems to be a physiological signaling molecule for several wound-and pathogeninduced responses (1). The conversion from fatty acid hydroperoxide to allene oxide in plants is catalyzed by a heme containing enzyme called allene oxide synthase (AOS) (2, 3). Plant AOS belongs to a subfamily of the fatty acid hydroperoxide metabolizing cytochrome P450s (P450s) designated as CYP74A (4 -6). Despite significant sequence homology of plant AOS to those of other P450s, the reaction of plant AOS is different from those of typical P450s (7,8). Plant AOS does not require the reductants and oxygen, and carries out the homolytic cleavage of the O-O bond in hydroperoxide, although typical P450s utilize two electrons and molecular oxygen for the hydroxylation of its substrate. Koljak et al. (1997) discovered and isolated a cDNA encoding a fusion protein of 8R-LOX and AOS from the Caribbean sea soft coral, Plexaura homomalla (9), the first example of an AOS found in animals. The fusion protein consists of a C-terminal 8R-LOX domain (79 kDa) and N-terminal heme-containing AOS domain (43 kDa). As shown in Scheme 1, reaction (i), the 8R-LOX domain initially catalyzes the oxygenation of arachidon...

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Section: Resultssupporting

confidence: 90%

On the Relationship of Coral Allene Oxide Synthase to Catalase

Tosha

Uchida

Brash

et al. 2006

Journal of Biological Chemistry

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“…Depolarization ratios were determined according to the procedure described in Materials and Methods. The assignment of EPO Raman bands was based on these depolarization ratios, on the observed dependence of signal intensities upon excitation wavelength, and on band assignments found in the literature for nickel(II)-octaethyl-porphyrinato (Abe et al, 1978), nickel(II)protoporphyrin IX, protoheme complexes (Choi et al, 1982a, b;, and protohemecontaining proteins like hemoglobin (Choi et al, 1982;Spiro, 1975;Spiro and Strekas, 1974), lactoperoxidase (Kitagawa et al, 1983;Manthey et al, 1986), horseradish peroxidase (Kitagawa et al, 1986;Terner et al, 1984) cytochrome c peroxidase (Smulevich et al, 1991b), intestinal peroxidase (Kimura et al, 1981), and different catalases (Sharma et al, 1989;Chuang, 1989).…”

Section: Assignment Of Raman Bandsmentioning

confidence: 87%

“…6 and 7). These lines are also very strong in spectra of pig intestinal Fe-S stretching mode at -350 cm-' (Champion, 1988 peroxidase (Kimura et al, 1981), lactoperoxidase (Manthey et al, 1986), and myeloperoxidase (Babcock et al, 1985), but absent or much less prominent in spectra of other protoporphyrin-IX proteins such as (leg)hemoglobin (Rousseau et al, 1983), myoglobin, horseradish peroxidase (Kitagawa et al, 1983), ferrous manganese peroxidase (Mino et al, 1988), chloroperoxidase (Bangcharoenpaurpong et al, 1986), and bovine liver ferric catalase (Chuang et al, 1989).…”

Section: Heme-protein Interactionsmentioning

confidence: 99%

Resonance Raman microspectroscopic characterization of eosinophil peroxidase in human eosinophilic granulocytes

Salmaso

Puppels

Caspers

et al. 1994

Biophysical Journal

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A resonance Raman microspectroscopic study is presented of eosinophil peroxidase (EPO) in human eosinophilic granulocytes. Experiments were carried out at the single cell level with laser excitation in Soret-, Qv-, and charge transfer absorption bands of the active site heme of the enzyme. The Raman signal obtained from the cells was almost exclusively due to EPO. Methods were developed to determine depolarization ratios and excitation profiles of Raman bands of EPO in situ. A number of Raman band assignments based on earlier experiments with isolated EPO have been revised. The results show that in agreement with literature on isolated eosinophil peroxidase, the prosthetic group of the enzyme in the (unactivated) cells is a high spin, 6-coordinated, ferric protoporphyrin IX. The core size of the heme is about 2.04 A. The proximal and distal axial ligands are most likely a histidine with the strong imidazolate character typical for peroxidases, and a weakly bound water molecule, respectively. The data furthermore indicate that the central iron is displaced from the plane of the heme ring. The unusual low wavenumber Raman spectrum of EPO, strongly resembling that of lactoperoxidase, intestinal peroxidase and myeloperoxidase, suggests that these mammalian peroxidases are closely related, and characterized by, as yet unspecified, interactions between the peripheral substituents and the protein, different from those found in other protoheme proteins.

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“…4B reveal a band at 518 cm −1 , which falls within this range. Much like the rR spectra of heme catalases [45], this band is insensitive to changes in pH from 6.4 to 9.7, indicating that it is not susceptible to axial ligand substitution by solvent and does not participate directly in acid–base reactions over this range. As in the case of ShuT [26], this behavior argues that the rR signature is not attributable to a hydroxide complex and that the 518-cm −1 band does not originate from an Fe–OH stretching mode.…”

Section: Discussionmentioning

confidence: 99%

Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor

Mokry

Nadia-Albete

Johnson

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background For many pathogenic microorganisms, iron acquisition represents a significant stress during the colonization of a mammalian host. Heme is the single most abundant source of soluble iron in this environment. While the importance of iron assimilation for nearly all organisms is clear, the mechanisms by which heme is acquired and utilized by many bacterial pathogens, even those most commonly found at sites of infection, remain poorly understood. Methods An alternative protocol for the production and purification of the outer membrane hemoglobin receptor (HmbR) from the pathogen Neisseria meningitidis has facilitated a biophysical characterization of this outer membrane transporter by electronic absorption, circular dichroism, electron paramagnetic resonance, and resonance Raman techniques. Results HmbR co-purifies with 5-coordinate high spin ferric heme bound. The heme binding site accommodates exogenous imidazole as a sixth ligand, which results in a 6-coordinate, low-spin ferric species. Both the 5- and 6-coordinate complexes are reduced by sodium hydrosulfite. Four HmbR variants with a modest decrease in binding efficiency for heme have been identified (H87C, H280A, Y282A, and Y456C). These findings are consistent with an emerging paradigm wherein the ferric iron center of bound heme is coordinated by a tyrosine ligand. Conclusion In summary, this study provides the first spectroscopic characterization for any heme or iron transporter in Neisseria meningitidis, and suggests a coordination environment heretofore unobserved in a TonB-dependent hemin transporter. General Significance A detailed understanding of the nutrient acquisition pathways in common pathogens such as N. meningitidis provides a foundation for new antimicrobial strategies.

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Resonance Raman spectra of bovine liver catalase: Enhancement of proximal tyrosinate vibrations

Cited by 23 publications

References 40 publications

On the Relationship of Coral Allene Oxide Synthase to Catalase

On the Relationship of Coral Allene Oxide Synthase to Catalase

Resonance Raman microspectroscopic characterization of eosinophil peroxidase in human eosinophilic granulocytes

Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor

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