Yeast cytochrome c-peroxidase

Peroxidases have also been utilized for preparative-scale oxidations of aromatic hydrocarbons. Procedures have been optimized for hydroxylation of l-tyrosine, D-(-)-p-hydroxyphenylglycine, and L-phenylalanine by oxygen, di-hydroxyfumaric acid, and horseradish peroxidase (89). Lactoperoxidase from bovine milk and yeast cytochrome c peroxidase will also catalyze such hydroxylation reactions (89). 

Bosshard HR, Anni H,YonetaniT (1991) Yeast cytochrome c peroxidase. In Everse J, Everse KE, Grisham MB (eds) Peroxidases in chemistry and biology. CRC Press, Boca Raton, p 51... 

Pig. 2. Comparison of the heme environments at the active sites of horse heart myoglobin 40) and yeast cytochrome c peroxidase 41). 

Figure 16-9 Stereoscopic a-carbon plot of yeast cytochrome c peroxidase (top) and yeast cytochrome c (below) as determined from a cocrystal by Pelletier and Kraut.164 The heme rings of the two proteins appear in bold lines, as does the ring of tryptophan 191 and the backbone of residues 191 — 193 of the cytochrome c peroxidase. Drawing from Miller et al.165...

Figure 16-13 The active site of yeast cytochrome c peroxidase. Access for substrates is through a channel above the front edge of the heme ring as viewed by the reader. A pathway for entrance of electrons may be via Trp 191 and His 175. From Holzbaur eta/.206 Based on coordinates of Finzel et al.215...

An analogous approach has been applied to study the electron transfer reaction between yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt c) by employing the complex between zinc-substituted CCP (ZnCCP) and native cyt c [70]. The two heme planes in this complex are nearly parallel at a metal-metal distance of 25 A and an edge-to-edge distance of 17-18 A. 

An analogous approach has been applied to study the electron transfer reaction between yeast cytochrome c peroxidase (CCP) and cytochrome c (cytc) by... 

Yeast cytochrome c peroxidase (CCP) is present in mitochondria and is induced under aerobic growth conditions. The enzyme preferentially oxidises cytochrome c, although small molecules can also act as substrates (De Pillis et al, 1991). The 1.7 A resolution... 

Fig. 5-4. Schematic structures of yeast cytochrome c peroxidase (CCP) and a highly basic horseradish isoperoxidase (HRP E5). The heme group shaded is seen nearly edge on with the iron atom indicated by a black dot. a-Helices are labelled A-J with a prime denoting additional helices present in HRP E5 but not in CCP. The position of cystine bridges (S - S), carbohydrate (Ch) and the amine (N) and carboxyl (C) termini are also indicated. Reproduced with permission from Welinder (1992).

Finzel BC, Poulos TL, Kraut J (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7 A resolution. J Biol Chem 259 13027-13036... 

Fig. 8. MCD spectra of ferryl iron. Low-temperature (50 or 100K) MCD spectra of ferryl iron in different proteins HRPCII, horse-radish peroxidase compound II HRPCX, horse-radish peroxidase compound X YCCP, yeast cytochrome c peroxidase compound I PsCCP, compound I of the dihaem cytochrome c peroxidase from Pseudomonas aeruginosa-, Mb pH 3.5, ferryl myoglobin formed at pH 3.5 MbpD9.0, the same compound found at pD9.0. Note the similarity of all the spectra with the exception of the alkaline form of ferryl myoglobin. Reprinted with permission from Cheesman, M.R., Greenwood, C. and Thomson, A.J. (1991) Adv. Inorg. Chem. 36, 201-255.

Yeast cytochrome c peroxidase (ferrocytochrome c hydrogen-peroxide oxidoreductase, EC 1.11.1.5) which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydroperoxide, was dls-... 

Erman, J. E., Vitello, L. B., Mauro, J. M., and Kraut, J., 1989, Detection of an oxy-ferryl porphyrin JC-cation radical in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I, Biochemistry 28 799297995. 

Mauro, J. M., Fishel, L. A., Hazzard, J. T., Meyer, T. E., Tollin, G., Cusanovich, M. A., and Kraut, J., 1988, Tryptophan-191-phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation. Biochemistry 27 6243n6256. 

Figure 1 (a) Schematic representation of yeast cytochrome c peroxidase (CcP) structure with heme and key active site residues represented as ball-and-stick models, (b) Active site architecture of yeast cytochrome c peroxidase (CcP) showing the role of all the key residues in catalysis. The dashed lines represent hydrogen bonds... 

Fig, 15. A schematic diagram illustrating the different two-electron oxidation processes undergone by Fe(III) hemes in horseradish peroxidase [Fe(IV)(por )], yeast cytochrome c peroxidase [Fe(IV(por)(R )], and diheme cytochrome c peroxidase. The porphyrin ring is represented by the square. Histidine is the proximal ligand in all cases. R represents an amino acid side chain. 

Mondal, M.S., Goodin, D.B., and Armstrong, F.A. (1998) Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high-potential catalytic states of wild-type and distal-pocket mutant (W51F) yeast cytochrome c peroxidase. Journal of the American Chemical Society, 120 (25), 6270-6276. 

Figure 4-6. (A) A close-up view of the active site of yeast cytochrome c peroxidase showing the residues in the distal pocket at which hydrogen peroxide is reduced to water. Overlaid on the structure of the wild type enzyme are the positions of residues in the W51F mutant (tryptophan is replaced by phenylalanine). (B) Voltammograms of a film of wild type CcP on a PGE electrode, obtained in the absence and presence of H2O2 at ice temperature, pH 5.0. The electrode is rotating at 200 rpm, but the catalytic current in this case continues to increase as the rotation rate is increased therefore under these conditions the electrocatalysis is diffusion controlled and few facts are revealed about the enzyme s chemistry. For the W51F mutant, the signal due to the reversible two-electron couple and the catalytic wave are both shifted >100 mV more positive in potential compared to the wild-type enzyme. Reproduced from ref. 46 and 47 with permission.

Fig. 1. Schematic diagram of yeast cytochrome c peroxidase C backbone generated from the X-ray coordinates il8) using Insight II (v. 2.3.0) software (BIOSYM Technologies Inc., San Diego). The heme, the distal His52, and the proximal Hisl75 are shown in bold.

Fig. 2. Active-site structure of yeast cytochrome c peroxidase. The dashed lines represent H-bonds between N1 of the distal His52 and the side-chain carbonyl of Asn82, and N1 of the proximal Hisl75 and the side-chain carboxylate of Asp235. This diagram was generated using the X-ray coordinates for the 1.7-A structure of CCP (18).

Metal Ions in Biological Systems Exploring Structure-Function Relationships in Yeast Cytochrome c Peroxidase Using Mutagenesis and Crystallography , Sigel,... 

Cytochrome c-550(s) was partially purified by Ketchum et al. (1969). Afterward it was purified to an electrophoretically homogeneous state (Yamanaka et al., 1982), and its complete amino acid sequence was determined (Tanaka et al., 1982). Its molecular mass is 12.4 kDa. The cytochrome is very similar to mitochondrial cytochrome c (similarity, 40% 19%) on the basis of the sequence, and reacts with yeast cytochrome c peroxidase at the rate of 79% as fast as mitochondrial cytochrome c. Ferrocytochrome c-550(s) is oxidized very fast with molecular oxygen by the catalysis of N. winogradskyi cytochrome c oxidase turnover number is 117 s 1 (Yamanaka et al., 1982 Nomoto et al., 1993). 

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