Resonance Raman Spectra of Native and Mesoheme-reconstituted Horseradish Peroxidase and Their Catalytic Intermediates

Kincaid, James R.; Zheng, Yaohua; Al-Mustafa, Jamil; Czarnecki, Kazimierz

doi:10.1074/jbc.271.46.28805

Cited by 53 publications

(48 citation statements)

References 41 publications

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“…The extended x-ray absorption fine structure and resonance Raman data reported for these systems are in good agreement with Badger's rule (6,(11)(12)(13)(16)(17)(18)(19), whereas the crystallographically determined bond distances deviate from it substantially (7-9). The long Fe-O bonds that have been reported in the crystal structures of these enzymes appear to be the hallmarks of ferric and ferrous hydroxides (14).…”

Section: Ron(iv)-hydroxides Have Been Implicated In the Catalyticsupporting

confidence: 71%

Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)–hydroxide

Stone

Behan

Green

2006

Proc. Natl. Acad. Sci. U.S.A.

104

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Section: Ron(iv)-hydroxides Have Been Implicated In the Catalyticsupporting

confidence: 71%

Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)–hydroxide

Stone

Behan

Green

2006

Proc. Natl. Acad. Sci. U.S.A.

104

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“…Since 2 , which primarily involves C b -C b stretching, is coupled with vinyl CϭC stretching (41,42), removal of the vinyl group leads to an increase in the frequency of 2 due to decoupling of the 2 and vinyl stretching modes (41)(42)(43). In fact, horseradish peroxidase reconstituted with mesoheme, which has ethyl groups instead of vinyl groups in the 2-and 4-positions of heme, showed an upshifted 2 at 1582 cm Ϫ1 as compared with that observed at 1573 cm Ϫ1 for native horseradish peroxidase (44). Previous studies have shown that the 2-vinyl mode has a more significant effect on the 2 frequency than the 4-vinyl (45).…”

mentioning

confidence: 95%

The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE

Uchida

Stevens

Daltrop

et al. 2004

Journal of Biological Chemistry

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The heme chaperone CcmE is a novel protein that binds heme covalently via a histidine residue as part of its essential function in the process of cytochrome c biogenesis in many bacteria as well as plant mitochondria. In the continued absence of a structure of the holoform of CcmE, identification of the heme ligands is an important step in understanding the molecular function of this protein and the role of covalent heme binding to CcmE during the maturation of c-type cytochromes. In this work, we present spectroscopic data that provide insight into the ligation of the heme iron in the soluble domain of CcmE from Escherichia coli. Resonance Raman spectra demonstrated that one of the heme axial ligands is a histidine residue and that the other is likely to be Tyr 134 . In addition, the properties of the heme resonances of the holo-protein as compared with those of a form of CcmE with non-covalently bound heme provide evidence for the modification of one of the heme vinyl side chains by the protein, most likely the 2-vinyl group.

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“…The Compound I species of CPO and HRP have sufficient half-lives for resonance Raman and EPR studies and have been well characterized (3,5,(15)(16)(17). The same peroxy acid and its derivatives have been used with P450s in attempts to generate intermediates.…”

mentioning

confidence: 99%

Kinetic Characterization of Compound I Formation in the Thermostable Cytochrome P450 CYP119

Kellner

Hung

Weiss

et al. 2002

Journal of Biological Chemistry

208

191

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P450 enzymes are ubiquitous in nature and carry out a wide range of important reactions including the activation of carbon centers for catabolism, steroid metabolism, and detoxification of xenobiotics (1). Due to the important physiological functions of P450 enzymes, the reaction intermediates of P450 chemistry have been a subject of investigation for many years. Several discreet steps occur in the hydroxylation chemistry of the cytochrome P450s including: substrate binding, first electron transfer to the P450 from a physiological redox partner, oxygen binding (to form oxy-P450), a second electron transfer event (to form a reduced oxy or peroxo state), proton transfer to the distal oxygen (forming hydroperoxo), and an oxygen scission event producing a putative high valent iron-oxo species that subsequently generates hydroxylated product (2). The high valent iron-oxo has long been thought to be analogous to the activated iron species characterized in other oxidative enzymes (horseradish peroxidase (HRP), 1 catalase, and chloroperoxidase (CPO)) and referred to as Compound I, a ferryl-oxo-() porphyrin cation radical (3-5). The intermediates in the complex P450 reaction cycle have been gradually divulged through the use of a wide range of spectroscopic techniques (6 -8) and the use of methods that allow access to the fast steps occurring after O 2 binding (2, 9). Recently the peroxo and hydroperoxo intermediates have been observed through the use of cryoenzymology techniques combined with radiolysis, generating these intermediates through gradual temperature annealing (2, 10). Although there has been no identification of a Compound I intermediate by these techniques, it has been inferred by indirect measurements (2,11,12). The Compound I state as well as the peroxo and hydroperoxo states of the enzyme have been proposed to be active in oxygenation events (13,14).To probe the nature of Compound I, meta-chloroperoxybenzoic acid (m-CPBA) has been used as an oxidizing agent to produce this high valent iron-oxo through heterolytic cleavage of the organic peroxide in CPO and HRP. The Compound I species of CPO and HRP have sufficient half-lives for resonance Raman and EPR studies and have been well characterized (3,5,(15)(16)(17). The same peroxy acid and its derivatives have been used with P450s in attempts to generate intermediates. Evidence for the existence of Compound I in P450s was demonstrated through substrate oxygenation or hydroxylation in the reaction of various organic peroxides with either liver microsomal P450 or CYP101, respectively (18,19,21).Contrary to the evidence for Compound I formation in cytochrome P450 using m-CPBA, Blake and Coon (20) reported that the reactions of several peroxy acids with CYP2B4 generated other active species, which are neither Compound I nor its one-electron-reduced adduct (Compound II). However, in previous studies the generation of the Compound I intermediate in cytochrome P450 (CYP101) required a large excess of peroxyacid, leading to the rapid formation, then conversion of ...

show abstract

Resonance Raman Spectra of Native and Mesoheme-reconstituted Horseradish Peroxidase and Their Catalytic Intermediates

Cited by 53 publications

References 41 publications

Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)–hydroxide

Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)–hydroxide

The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE

Kinetic Characterization of Compound I Formation in the Thermostable Cytochrome P450 CYP119

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