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Page 1
Crystal structure of nitric oxide inhibited cytochrome c peroxidase.
Edwards SL, Kraut J, Poulos TL. Edwards SL, et al. Among authors: kraut j. Biochemistry. 1988 Oct 18;27(21):8074-81. doi: 10.1021/bi00421a016. Biochemistry. 1988. PMID: 2852951
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, 8199-82 …
As a model for the substrate hydrogen peroxide, this geometry is consistent with the suggestion that Arg-48 serves to polarize the O-O perox …
X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis.
Wang JM, Mauro M, Edwards SL, Oatley SJ, Fishel LA, Ashford VA, Xuong NH, Kraut J. Wang JM, et al. Among authors: kraut j. Biochemistry. 1990 Aug 7;29(31):7160-73. doi: 10.1021/bi00483a003. Biochemistry. 1990. PMID: 2169873
The 2.2-A X-ray structure for CCP(MI), a plasmid-encoded form of Saccharomyces cerevisiae cytochrome c peroxidase (CCP) expressed in Escherichia coli [Fishel, L.A., Villafranca, J. E., Mauro, J. M., & Kraut, J. (1987) Biochemistry 26, 351-360], has …
The 2.2-A X-ray structure for CCP(MI), a plasmid-encoded form of Saccharomyces cerevisiae cytochrome c peroxidase (CCP) expressed in Escheri …
Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c.
Miller MA, Hazzard JT, Mauro JM, Edwards SL, Simons PC, Tollin G, Kraut J. Miller MA, et al. Among authors: kraut j. Biochemistry. 1988 Dec 27;27(26):9081-8. doi: 10.1021/bi00426a003. Biochemistry. 1988. PMID: 2853973
The long-distance electron transfer observed in the complex formed between ferrocytochrome c and compound I, the peroxide-oxidized form of cytochrome c peroxidase (CCP), has been proposed to occur through the participation of His 181 of CCP and Phe 87 of yeast iso-1 cytochrome c …
The long-distance electron transfer observed in the complex formed between ferrocytochrome c and compound I, the peroxide-oxidized form of c …
Crystal structure of cytochrome c peroxidase compound I.
Edwards SL, Nguyen HX, Hamlin RC, Kraut J. Edwards SL, et al. Among authors: kraut j. Biochemistry. 1987 Mar 24;26(6):1503-11. doi: 10.1021/bi00380a002. Biochemistry. 1987. PMID: 3036202
These observations, together with the results of mutagenesis experiments [Fishel, L. A., Villafranca, J. E., Mauro, J. M., & Kraut, J. (1987) Biochemistry 26, 351-360; Goodin, D. B., Mauk, A. ...
These observations, together with the results of mutagenesis experiments [Fishel, L. A., Villafranca, J. E., Mauro, J. M., &am …
Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.
Mauro JM, Fishel LA, Hazzard JT, Meyer TE, Tollin G, Cusanovich MA, Kraut J. Mauro JM, et al. Among authors: kraut j. Biochemistry. 1988 Aug 23;27(17):6243-56. doi: 10.1021/bi00417a008. Biochemistry. 1988. PMID: 2851317
On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be important in determining the spectroscopic and catalytic properties of the enzyme [Edwards, S. L., Xuong, Ng. H., Hamlin, R. C., & Kra …
On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be i …
286 results