In vitro studies on yeast cytochrome c peroxidase and its possible function in the electron transfer and energy coupling reactions

Erecińska, Maria; Oshino, Nozomu; Loh, Ping Yeap; Brocklehurst, Elizabeth

doi:10.1016/0005-2728(73)90245-4

Cited by 41 publications

(6 citation statements)

References 21 publications

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“…Similarity of structure between CCP and the globins was suggested by the fact that certain heme-binding inhibitors of myoglobin and hemoglobin, including nitric oxide, also inhibit CCP to yield complexes with absorption spectra similar to those of inhibited globin complexes (Yonetani & Ray, 1965). Moreover, CCP has been shown to be able to substitute for the terminal oxidase in yeast when the latter is inactivated by carbon monoxide (Erecinska et al, 1973). These properties of CCP, including its ease of crystallization, recommend it as a model for the study of cytochrome oxidase, which is more complicated and difficult to crystallize.…”

mentioning

confidence: 88%

Crystal structure of nitric oxide inhibited cytochrome c peroxidase

Edwards

Kraut²,

Poulos³

1988

Biochemistry

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We have collected X-ray diffraction data from a crystal of cytochrome c peroxidase (CCP) complexed with the inhibitor nitric oxide to a resolution of 2.55 A. A difference Fourier map shows density indicating the NO ligand is bound to the heme iron at the sixth coordination site in a bent configuration. Structural adjustments were determined by least-squares refinement that yielded an agreement residual of R = 0.18. The orientation of the ligand, tilting toward Arg-48, causes adjustment in the position of this nearby polar side chain. As a model for the substrate hydrogen peroxide, this geometry is consistent with the suggestion that Arg-48 serves to polarize the O-O peroxide bond to promote heterolytic cleavage of the bond [Poulos, T. L., & Kraut, J. (1980) J. Biol. Chem. 255, 8199-8205]. Strong difference density is also observed near residues 190-194, especially around the indole ring of Trp-191. The density indicates movement of the indole ring away from the proximal His-175 imidazole ring by about 0.25 A, which appears to cause perturbation of the neighboring residues. The response of Trp-191 on the proximal side of the heme to binding nitric oxide on the distal side probably results from delocalization of the electron density of the ligand. Relevant to this is the recent finding that a mutant in which Trp-191 is replaced by phenylalanine has dramatically reduced activity, less than 0.05% of the parent activity [Mauro, J. M., Fishel, L. A., Hazzard, J. T., Meyer, T. E., Tollin, G., Cusanovich, M. A., & Kraut, J. (1988) Biochemistry 27, 6243-6256].(ABSTRACT TRUNCATED AT 250 WORDS)

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mentioning

confidence: 88%

Crystal structure of nitric oxide inhibited cytochrome c peroxidase

Edwards

Kraut²,

Poulos³

1988

Biochemistry

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“…In control experiments using 3-amino-1,2,4-triazole, staining of peroxisomes was not observed, indicating that the cytochemical staining of peroxisomes was the result of catalase activity (Van Dijken et al 1975;Veenhuis et al 1976;Hänssler et al 1981). In addition, staining of mitochondria with the diaminobenzidine procedure was frequently observed as the result of the peroxidative reaction of cytochrome c peroxidase or other mitochondrial haem protein (Hoffman et al 1970;Todd and Vigil 1972;Erecinska et al 1973).…”

Section: Strainmentioning

confidence: 98%

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Lucas

Valenciano

Domínguez

et al. 1997

Archives of Microbiology

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Conidia of Aspergillus nidulans were mutagenized with ultraviolet light and were incubated on a special selective medium containing the catalase inhibitor 3-amino-1,2,4-triazole. From approximately 5 x 10(7) viable UV-irradiated conidia tested, 423 stable mutants resistant to 3-amino-1,2,4-triazole were recovered, of which 40 were unable to grow on minimal medium with oleic acid as the sole carbon source. These oleate-nonutilizing (Ole-) mutants did not grow on medium with carbon sources requiring functional peroxisomes (oleate, butyrate, acetate, or ethanol), but grew well on medium with carbon sources supposedly not requiring such organelles (glucose, glycerol, l-glutamate, or l-proline). The Ole- mutants carried mutations in one of five nuclear genes affecting acetate utilization: acuJ, acuH, acuE, acuL, and perA. The perA21 strain (DL21) carried a mutation in a gene that is not allelic with any of the known acu loci and displayed a phenotype resembling that described in the Pim- (peroxisome import defective) mutants of Hansenula polymorpha. Hyphae of the perA21 mutant contained a few small peroxisomes with the bulk of peroxisomal enzymes remaining in the 20,000 x g supernatant, but produced wild-type levels of penicillin.

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“…However, in these experiments as well as in incubations with DAB and H202 or with oxidized DAB, accumulation of the stain in mitochondria was apparent. This may be due to staining of cytochrome c peroxidase, which is located in the mitochondria (Hoffman et al, 1970;Todd and Vigil, 1972;Erecifiska et al, 1973). Incubations of unfixed cells with DAB and different concentrations of H202 always resulted in unstained peroxisomes.…”

Section: Staining Of Catalase With Dab and Hydrogen Peroxidementioning

confidence: 99%