Formation and photolability of low-spin ferrous cytochrome c peroxidase at alkaline pH

Wang, Jianling; Boldt, Nancy J.; Ondrias, M. R.

doi:10.1021/bi00118a032

Cited by 15 publications

(22 citation statements)

References 42 publications

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“…2B. These values suggest that ferrous OxdB includes a five-coordinated high-spin heme [15][16][17][18][19]. These results are consistent with those of electronic absorption spectra.…”

Section: Resonance Raman Spectrasupporting

confidence: 75%

“…2A. These bands are typical of six-coordinated high-spin hemes [15][16][17][18][19]. Marker bands of ferrous OxdB were observed at m 2 = 1566, m 3 = 1473, and m 4 = 1357 cm À1 , as shown in Fig.…”

Section: Resonance Raman Spectramentioning

confidence: 96%

“…2C and D). Marker bands of ferric OxdRE appeared at m 2 = 1574, m 3 = 1503, and m 4 = 1374 cm À1 , which can be assigned to a six-coordinated low-spin heme [15,[18][19][20]. Ferrous OxdRE exhibited marker bands typical of a five-coordinated high-spin heme at m 2 = 1558, m 3 = 1473, and m 4 = 1359 cm À1 , as shown in Fig.…”

Section: Resonance Raman Spectramentioning

confidence: 98%

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Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE

Kobayashi¹,

Pal²,

Shiro³

et al. 2006

Journal of Inorganic Biochemistry

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“…2B. These values suggest that ferrous OxdB includes a five-coordinated high-spin heme [15][16][17][18][19]. These results are consistent with those of electronic absorption spectra.…”

Section: Resonance Raman Spectrasupporting

confidence: 75%

Section: Resonance Raman Spectramentioning

confidence: 96%

See 1 more Smart Citation

Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE

Kobayashi¹,

Pal²,

Shiro³

et al. 2006

Journal of Inorganic Biochemistry

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“…The ν 4 oxidation state marker at 1360 cm −1 is characteristic of a ferrous heme. The spin state marker ν 3 has one main contribution at 1475 cm −1 , indicating a 5-c, HS ferrous heme [38], consistent with the absorption spectrum with a Soret band at 439 nm and Q-bands at 554 and 593 nm (data not shown) of a 5-c, HS ferrous heme [52]. A small, residual contribution of ferric 5-c, QS heme cannot be excluded as indicated by a weak ν 3 mode at 1500 cm −1 , which is similar to our observations after reduction of WT KatG [51].…”

Section: Ferrous Katg(y229f)supporting

confidence: 69%

Modification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met–Tyr–Trp cross-linked adduct

Kapetanaki

Zhao

et al. 2007

Journal of Inorganic Biochemistry

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Mycobacterium tuberculosis catalase-peroxidase (Mtb KatG) is a bifunctional enzyme that possesses both catalase and peroxidase activities and is responsible for the activation of the antituberculosis drug isoniazid. Mtb KatG contains an unusual adduct in its distal heme pocket that consists of the covalently linked Trp107, Tyr229, and Met255. The KatG(Y229F) mutant lacks this adduct and has decreased steady-state catalase activity and enhanced peroxidase activity. In order to test a potential structural role of the adduct that supports catalase activity, we have used resonance Raman spectroscopy to probe the local heme environment of KatG(Y229F). In comparison to wild-type KatG, resting KatG(Y229F) contains a significant amount of 6-coordinate, low-spin heme and a more planar heme. Resonance Raman spectroscopy of the ferrous-CO complex of KatG(Y229F) suggest a non-linear Fe-CO binding geometry that is less tilted than in wild-type KatG. These data provide evidence that the Met-Tyr-Trp adduct imparts structural stability to the active site of KatG that seems to be important for sustaining catalase activity.

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“…Cytochrome c peroxidase (CcP) was extracted from bakers' yeast and crystallized by a modified procedure (9). Myoglobin (horse skeletal) was purchased from Sigma and used without further purification.…”

mentioning

confidence: 99%

Identification of the overtone of the Fe-CO stretching mode in heme proteins: a probe of the heme active site.

Wang

Takahashi

Rousseau

1995

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

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Two CO-isotope sensitive lines have been detected in the overtone region of the resonance Raman spectra of CO-bound hemeproteins. One line is assigned as the overtone of the Fe-CO stretching mode and is located in the 1000-to 1070-cm'1 region. The other line is found in the 1180-to 1210-cmn-' region and is assigned as a combination between a porphyrin mode, V7, and the F6-CO stretching mode. The high intensities of these lines, which in the terminal oxidase class of proteins are of the same order as those of the fundamental stretching mode, indicate that the mechanism of enhancement for modes involving the Fe-CO moiety is different from that for the modes of the porphyrin macrocycle and call for reexamination of Raman theory of porphyrins as applied to axial ligands. The anharmonicity of the electronic potential function was evaluated, revealing that in the terminal oxidases the anharmonicity is greater than in the other heme proteins that were examined, suggesting a distinctive interaction of the bound CO with its distal environment in this family. Furthermore, the anharmonicity correlates with the frequency of the C-0 stretching mode, demonstrating that both of these parameters are sensitive to the Fe-CO bond energy. The overtone and combination lines involving the bound CO promise to be additional probes of heme protein structural properties.Heme proteins, which function either as oxygen carriers or as catalytic enzymes, have a pocket on the distal side of the heme in which exogenous ligands bind to the iron atom. The function of the heme protein depends critically on the properties of the distal pocket and how its residues interact with the hemebound exogenous ligands. Studies of CO adducts of heme proteins have been shown to be extremely important probes of the active sites, including the interactions between the CO and the distal residues (1, 2). In addition, CO photodissociation and recombination studies have played an essential role in unraveling the dynamic processes that occur in heme proteins, information which has led to an advanced understanding of the basic physics that forms the foundation of the physiological process of ligand binding (3, 4).Structural information such as the identity of the proximal ligand, the geometry of the bound CO, and the interactions between the axial ligands and the heme environment has been determined from the vibrational spectra of the fundamental modes involving the CO. However, overtones offer the possibility of yielding additional information concerning the heme pocket and the electronic structure because the behavior of the overtones depends critically on the shape of the ground-state potential function as well as the properties of the excited electronic state. In the overtone region of the Fe-CO stretching mode ("Feco) two lines have been independently discovered recently (5, 6). We assign one as the overtone ("over) Of the Fe-CO stretching mode and the second as a combination (Vcomb) of the Fe-CO stretching mode with a mode of the porphyrin macrocycle (V7...

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Formation and photolability of low-spin ferrous cytochrome c peroxidase at alkaline pH

Cited by 15 publications

References 42 publications

Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE

Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE

Modification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met–Tyr–Trp cross-linked adduct

Identification of the overtone of the Fe-CO stretching mode in heme proteins: a probe of the heme active site.

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