Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states

Smulevich, Giulietta; Evangelista-Kirkup, Ruby; English, Ann M.; Spiro, Thomas G.

doi:10.1021/bi00363a038

Cited by 68 publications

(72 citation statements)

References 14 publications

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“…Our results reveal that a 5-c heme form of KatG may be isolated but that coordination and spin state changes are unavoidable during handling of the enzyme under a variety of conditions. Similar issues have appeared in the literature over the years concerning yeast CCP (25)(26)(27)(28).…”

supporting

confidence: 66%

Analysis of Heme Structural Heterogeneity in Mycobacterium tuberculosis Catalase-Peroxidase (KatG)

Chouchane

Girotto

Kapetanaki

et al. 2003

Journal of Biological Chemistry

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Mycobacterium tuberculosis catalase-peroxidase (KatG) is a heme enzyme considered important for virulence, which is also responsible for activation of the anti-tuberculosis pro-drug isoniazid. Here, we present an analysis of heterogeneity in KatG heme structure using optical, resonance Raman, and EPR spectroscopy. Examination of ferric KatG under a variety of conditions, including enzyme in the presence of fluoride, chloride, or isoniazid, and at different stages during purification in different buffers allowed for assignment of spectral features to both five-and six-coordinate heme. Five-coordinate heme is suggested to be representative of "native" enzyme, since this species was predominant in the enzyme examined immediately after one chromatographic protocol. Quantum mechanically mixed spin heme is the most abundant form in such partially purified enzyme. Reduction and reoxidation of sixcoordinate KatG or the addition of glycerol or isoniazid restored five-coordinate heme iron, consistent with displacement of a weakly bound distal water molecule. The rate of formation of KatG Compound I is not retarded by the presence of six-coordinate heme either in wild-type KatG or in a mutant (KatG[Y155S]) associated with isoniazid resistance, which contains abundant six-coordinate heme. These results reveal a number of similarities and differences between KatG and other Class I peroxidases.

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supporting

confidence: 66%

Analysis of Heme Structural Heterogeneity in Mycobacterium tuberculosis Catalase-Peroxidase (KatG)

Chouchane

Girotto

Kapetanaki

et al. 2003

Journal of Biological Chemistry

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“…Franzen therefore proposes that the ν CO stretch for Fe(II) heme proteins is sensitive to the histidinate character of the trans axial His, and should decrease as His − increases 73. Consistent with this proposal, comparison of the Fe(II)-CO vibrational frequencies of HRP relative to CcP reveals that the lower potential peroxidase (HRP) exhibits higher ν FeC and lower ν CO 7,70,76–77. In recent DFT results by Daskalakis and Varotsis, however, it was determined that the ν CO changes for model complexes can be quite small for slight variations in His − character 71.…”

Section: Discussionmentioning

confidence: 85%

Variation and Analysis of Second-Sphere Interactions and Axial Histidinate Character inc-type Cytochromes

Bowman

Bren

2010

Inorg. Chem.

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The electron-donating properties of the axial His ligand to heme iron in cytochromes c (cyts c) are found to be correlated with midpoint reduction potential (E m ) in variants of Hydrogenobacter thermophilus cytochrome c 552 (Ht cyt c 552 ) in which mutations have been made in and near the Cys-X-X-Cys-His (CXXCH) heme-binding motif. To probe the strength of the His-Fe(III) interaction, we have measured 13 C nuclear magnetic resonance (NMR) chemical shifts for 13 CN − bound to heme iron trans to the axial His in Ht Fe(III) cyt c 552 variants. We observe a linear relationship between these 13 C chemical shifts and E m , indicating that the His-Fe(III) bond strength correlates with E m . To probe a conserved hydrogen bonding interaction between the axial His Hδ1 and the backbone carbonyl of a Pro residue, we measured the pK a of the axial His Hδ1 proton (pK a(2) ), which we propose to relate to the His-Fe(III) interaction, reduction potential and local electrostatic effects. The observed linear relationship between the axial His 13 Cβ chemical shift and E m is proposed to reflect histidinate (anionic) character of the ligand. A linear relationship also is seen between the average heme methyl 1 H chemical shift and E m which may reflect variation in axial His electron-donating properties or in the ruffling distortion of the heme plane. In summary, chemical shifts of the axial His and exogenous CN − bound trans to His are shown to be sensitive probes of the His-Fe(III) interaction in variants of Ht cyt c 552 and display trends that correlate with E m .

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“…The backbonding correlation, a plot of Fe–CO stretching versus C–O stretching vibrational frequencies, is a useful tool for identifying a proximal ligand262728. Fig.…”

Section: Resultsmentioning

confidence: 99%

“…2C)262728. The lower line corresponds to the proteins with neutral proximal ligands that are bound to the heme iron through a histidine residue.…”

Section: Resultsmentioning

confidence: 99%

Identification of Essential Histidine Residues Involved in Heme Binding and Hemozoin Formation in Heme Detoxification Protein from Plasmodium falciparum

Nakatani

Ishikawa

Aono

et al. 2014

Sci Rep

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Malaria parasites digest hemoglobin within a food vacuole to supply amino acids, releasing the toxic product heme. During the detoxification, toxic free heme is converted into an insoluble crystalline form called hemozoin (Hz). Heme detoxification protein (HDP) in Plasmodium falciparum is one of the most potent of the hemozoin-producing enzymes. However, the reaction mechanisms of HDP are poorly understood. We identified the active site residues in HDP using a combination of Hz formation assay and spectroscopic characterization of mutant proteins. Replacement of the critical histidine residues His122, His172, His175, and His197 resulted in a reduction in the Hz formation activity to approximately 50% of the wild-type protein. Spectroscopic characterization of histidine-substituted mutants revealed that His122 binds heme and that His172 and His175 form a part of another heme-binding site. Our results show that the histidine residues could be present in the individual active sites and could be ligated to each heme. The interaction between heme and the histidine residues would serve as a molecular tether, allowing the proper positioning of two hemes to enable heme dimer formation. The heme dimer would act as a seed for the crystal growth of Hz in P. falciparum.

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Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states

Cited by 68 publications

References 14 publications

Analysis of Heme Structural Heterogeneity in Mycobacterium tuberculosis Catalase-Peroxidase (KatG)

Analysis of Heme Structural Heterogeneity in Mycobacterium tuberculosis Catalase-Peroxidase (KatG)

Variation and Analysis of Second-Sphere Interactions and Axial Histidinate Character inc-type Cytochromes

Identification of Essential Histidine Residues Involved in Heme Binding and Hemozoin Formation in Heme Detoxification Protein from Plasmodium falciparum

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