cytochrome c peroxidase

Summary

Summary: A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC 1.11.1.5.

Top Publications

  1. Arciero D, Hooper A. A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states. J Biol Chem. 1994;269:11878-86 pubmed
    ..This suggests that this di-heme peroxidase may form a compound I intermediate analogous to that formed by horseradish peroxidase...
  2. Karlsen O, Larsen Ø, Jensen H. Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8. Microbiology. 2010;156:2682-90 pubmed publisher
    ..sequence deduced from this gene showed significant sequence similarity to the surface-associated di-haem cytochrome c peroxidase (SACCP) previously isolated from Methylococcus capsulatus (Bath), including both c-type haem-binding ..
  3. Daum G, Böhni P, Schatz G. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J Biol Chem. 1982;257:13028-33 pubmed
    ..Cytochrome b2 and cytochrome c peroxidase were found to be components of the intermembrane space...
  4. Dantas A, Andrade R, de Carvalho M, Felipe M, Campos E. Oxidative stress response in Paracoccidioides brasiliensis: assessing catalase and cytochrome c peroxidase. Mycol Res. 2008;112:747-56 pubmed publisher
    ..brasiliensis has a powerful antioxidant defence system enabling it to survive H(2)O(2)-mediated stress...
  5. Karlsen O, Kindingstad L, Angelskår S, Bruseth L, Straume D, Puntervoll P, et al. Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins. FEBS J. 2005;272:6324-35 pubmed
    ..MCA2590-encoded protein shared significant, but restricted, sequence similarity to the bacterial di-heme cytochrome c peroxidase (BCCP) family of proteins...
  6. Musah R, Jensen G, Bunte S, Rosenfeld R, Goodin D. Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein. J Mol Biol. 2002;315:845-57 pubmed
    ..Here, the binding of compounds to the W191G cavity mutant of cytochrome c peroxidase is characterized by X-ray crystallography and binding thermodynamics...
  7. Morar A, Wang X, Pielak G. Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory. Biochemistry. 2001;40:281-5 pubmed
    ..None of the analyses are completely successful by themselves, and the results suggest that a complete analysis must account for both excluded-volume and chemical interactions. ..
  8. Charizanis C, Juhnke H, Krems B, Entian K. The mitochondrial cytochrome c peroxidase Ccp1 of Saccharomyces cerevisiae is involved in conveying an oxidative stress signal to the transcription factor Pos9 (Skn7). Mol Gen Genet. 1999;262:437-47 pubmed
    ..fap24, which was respiration-competent, could be complemented by CCP1, which encodes the mitochondrial cytochrome c peroxidase. Mitochondrial cytochrome c peroxidase degrades reactive oxygen species within the mitochondria...
  9. Pauleta S, Lu Y, Goodhew C, Moura I, Pettigrew G, Shelnutt J. Calcium-dependent conformation of a heme and fingerprint peptide of the diheme cytochrome c peroxidase from Paracoccus pantotrophus. Biochemistry. 2001;40:6570-9 pubmed
    The structural changes in the heme macrocycle and substituents caused by binding of Ca(2+) to the diheme cytochrome c peroxidase from Paracoccus pantotrophus were clarified by resonance Raman spectroscopy of the inactive fully oxidized ..

More Information

Publications62

  1. Turner S, Reid E, Smith H, Cole J. A novel cytochrome c peroxidase from Neisseria gonorrhoeae: a lipoprotein from a Gram-negative bacterium. Biochem J. 2003;373:865-73 pubmed
    A cytochrome c peroxidase (CCP) produced by Neisseria gonorrhoeae has been shown to have novel characteristics by investigating its location, expression and role in Neisseria gonorrhoeae and by expression in Escherichia coli...
  2. De Smet L, Savvides S, Van Horen E, Pettigrew G, Van Beeumen J. Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases. J Biol Chem. 2006;281:4371-9 pubmed
    ..Our results help to clarify a number of aspects of the debate on structure-function relationships in this family of bacterial CCPs and set the stage for future studies. ..
  3. Fulop V, Ridout C, Greenwood C, Hajdu J. Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Structure. 1995;3:1225-33 pubmed
    b>Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis...
  4. Suppanz I, Wurm C, Wenzel D, Jakobs S. The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell. 2009;20:572-80 pubmed publisher
    ..We have analyzed the localizations of the m-AAA protease and its substrate cytochrome c peroxidase (Ccp1) within yeast mitochondria using live cell fluorescence microscopy and quantitative immunoelectron ..
  5. Baron R, McCammon J. Dynamics, hydration, and motional averaging of a loop-gated artificial protein cavity: the W191G mutant of cytochrome c peroxidase in water as revealed by molecular dynamics simulations. Biochemistry. 2007;46:10629-42 pubmed
    Five molecular dynamics simulations of the W191G cavity mutant of cytochrome c peroxidase in explicit water reveal distinct dynamic and hydration behavior depending on the closed or open state of the flexible loop gating the cavity, the ..
  6. Hoffmann M, Seidel J, Einsle O. CcpA from Geobacter sulfurreducens is a basic di-heme cytochrome c peroxidase. J Mol Biol. 2009;393:951-65 pubmed publisher
  7. Partridge J, Poole R, Green J. The Escherichia coli yhjA gene, encoding a predicted cytochrome c peroxidase, is regulated by FNR and OxyR. Microbiology. 2007;153:1499-507 pubmed
    ..coli yhjA gene. The yhjA gene encodes a predicted cytochrome c peroxidase, a bacterial haem-containing protein involved in the peroxide stress response through its ability to ..
  8. Dabir D, Leverich E, Kim S, Tsai F, Hirasawa M, Knaff D, et al. A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1. EMBO J. 2007;26:4801-11 pubmed
    ..oxygen as an electron acceptor to generate hydrogen peroxide, which is subsequently reduced to water by cytochrome c peroxidase (Ccp1). Oxidized Ccp1 was in turn reduced by the Erv1-reduced cytochrome c...
  9. Samyn B, Van Craenenbroeck K, De Smet L, Vandenberghe I, Pettigrew G, Van Beeumen J. A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase. FEBS Lett. 1995;377:145-9 pubmed
    The amino acid sequence of cytochrome c peroxidase from Pseudomonas aeruginosa has been determined using classical chemical degradation techniques combined with accurate mass analysis of all the generated peptides...
  10. Kathiresan M, English A. LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H2O2. Chem Sci. 2017;8:1152-1162 pubmed publisher
    We recently reported that cytochrome c peroxidase (Ccp1) functions as a H2O2 sensor protein when H2O2 levels rise in respiring yeast...
  11. Thorsen T, Maerkl S, Quake S. Microfluidic large-scale integration. Science. 2002;298:580-4 pubmed
    ..We used these integrated microfluidic networks to construct the microfluidic analog of a comparator array and a microfluidic memory storage device whose behavior resembles random-access memory. ..
  12. Jain R, Ernst J, Kutzki O, Park H, Hamilton A. Protein recognition using synthetic surface-targeted agents. Mol Divers. 2004;8:89-100 pubmed
    ..In this way strong and selective binding to a protein surface has be achieved and disruption of clinically important protein-protein interactions has been demonstrated in models of human disease. ..
  13. Kathiresan M, English A. Targeted proteomics identify metabolism-dependent interactors of yeast cytochrome c peroxidase: implications in stress response and heme trafficking. Metallomics. 2016;8:434-43 pubmed publisher
    Recently we discovered that cytochrome c peroxidase (Ccp1) functions primarily as a mitochondrial H2O2 sensor and heme donor in yeast cells...
  14. Zarić S, Popovic D, Knapp E. Factors determining the orientation of axially coordinated imidazoles in heme proteins. Biochemistry. 2001;40:7914-28 pubmed
    ..orientations of axially coordinated imidazoles for all groups of heme proteins, except for the group of cytochrome c peroxidase. In this group, the orientation of the imidazole is determined by a strong hydrogen bond of the NdeltaH ..
  15. Kang S, Hoke K, Crane B. Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films. J Am Chem Soc. 2006;128:2346-55 pubmed
    D(2)O-grown crystals of yeast zinc porphyrin substituted cytochrome c peroxidase (ZnCcP) in complex with yeast iso-1-cytochrome c (yCc) diffract to higher resolution (1.7 A) and pack differently than H(2)O-grown crystals (2.4-3.0 A)...
  16. Gonchar M, Kostryk L, Sibirny A. Cytochrome c peroxidase from a methylotrophic yeast: physiological role and isolation. Appl Microbiol Biotechnol. 1997;48:454-8 pubmed
    ..strains is strongly correlated with increased levels of the alternative H2O2-destroying enzyme, cytochrome c peroxidase. Cytochrome c peroxidase from cell-free extracts of one of the scd revertants has been purified to ..
  17. Moon H, Baek D, Lee B, Prasad D, Lee S, Cho M, et al. Soybean ascorbate peroxidase suppresses Bax-induced apoptosis in yeast by inhibiting oxygen radical generation. Biochem Biophys Res Commun. 2002;290:457-62 pubmed
    ..H(2)O(2)-sensitive phenotype of yeast cytosolic catalase T (Deltactt)- and thermosensitive phenotype of cytochrome c peroxidase (Deltaccp)-deleted mutant cells...
  18. Bingham Ramos L, Hendrixson D. Characterization of two putative cytochrome c peroxidases of Campylobacter jejuni involved in promoting commensal colonization of poultry. Infect Immun. 2008;76:1105-14 pubmed
    ..We previously found that a mutant lacking docA, which encodes a putative cytochrome c peroxidase (CCP), demonstrates up to a 10(5)-fold reduction in colonization of the chick cecum compared to wild-type ..
  19. Green M. Application of Badger's rule to heme and non-heme iron-oxygen bonds: an examination of ferryl protonation states. J Am Chem Soc. 2006;128:1902-6 pubmed
    ..have been reported in the crystal structures of the ferryl forms of myoglobin, horseradish peroxidase, cytochrome c peroxidase, and catalase deviate substantially from the values predicted by Badger's rule, while the short Fe-O ..
  20. Barrows T, Bhaskar B, Poulos T. Electrostatic control of the tryptophan radical in cytochrome c peroxidase. Biochemistry. 2004;43:8826-34 pubmed
    Previously a K(+)-binding site, analogous to that found in ascorbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP) to test the hypothesis that the bound K(+) influences the stability of the Trp191 cation radical ..
  21. Hoffman B, Celis L, Cull D, Patel A, Seifert J, Wheeler K, et al. Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface. Proc Natl Acad Sci U S A. 2005;102:3564-9 pubmed
    ..for this proposal in measurements on (i) mixed-metal hemoglobin hybrids, (ii) the complex between cytochrome c peroxidase and cytochrome c, and (iii and iv) the complexes of myoglobin and isolated hemoglobin alpha-chains with ..
  22. Muench D, Kuch D, Wu H, Begum A, Veit S, Pelletier M, et al. Hydrogen peroxide-producing lactobacilli inhibit gonococci in vitro but not during experimental genital tract infection. J Infect Dis. 2009;199:1369-78 pubmed publisher
    ..crispatus. A gonococcal catalase mutant and a catalase, cytochrome C peroxidase mutant exhibited greater susceptibility to L...
  23. Ronnberg M. Amino acid sequences of the two heme c-binding sites of Pseudomonas cytochrome-c peroxidase. Biochim Biophys Acta. 1987;912:82-6 pubmed
  24. Satterlee J, Teske J, Erman J, Mauro J, Poulos T. Temperature, pH, and solvent isotope effects on cytochrome c peroxidase mutant N82A studied by proton NMR. J Protein Chem. 2000;19:535-42 pubmed
    The mutant of baker's yeast cytochrome c peroxidase-CN with Ala82 in place of Asn82, [N82A]CcPCN, exhibits a complex solution behavior featuring dynamic interconversion among three enzyme forms that so far have only been detected by NMR ..
  25. Moore G, Cox M, Crowe D, Osborne M, Rosell F, Bujons J, et al. N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J. 1998;332 ( Pt 2):439-49 pubmed
    ..for use as NMR probes of the complexes formed by cytochrome c with bovine liver cytochrome b5 and yeast cytochrome c peroxidase. The electrostatic properties and structures of the derivatized cytochromes are not significantly ..
  26. Scalinci S, Scorolli L, De Martino L, Corazza D, Morara M, Meduri R. Effect of cytochrome c peroxidase on corneal epithelial healing process after photorefractive keratectomy. J Cataract Refract Surg. 2005;31:1928-31 pubmed
    To evaluate the role of commercially prepared cytochrome c peroxidase eyedrops in corneal epithelial healing after photorefractive keratectomy (PRK)...
  27. Bender T, Leidhold C, Ruppert T, Franken S, Voos W. The role of protein quality control in mitochondrial protein homeostasis under oxidative stress. Proteomics. 2010;10:1426-43 pubmed publisher
    ..As Pim1/LON expression was induced significantly under ROS treatment, we propose that this protease system performs a crucial protective function under oxidative stress conditions. ..
  28. Nakani S, Viriyakul T, Mitchell R, Vitello L, Erman J. Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase. Biochemistry. 2006;45:9887-93 pubmed
    A covalent complex between recombinant yeast iso-1-cytochrome c and recombinant yeast cytochrome c peroxidase (rCcP), in which the crystallographically defined cytochrome c binding site [Pelletier, H., and Kraut, J...
  29. Sharp K, Mewies M, Moody P, Raven E. Crystal structure of the ascorbate peroxidase-ascorbate complex. Nat Struct Biol. 2003;10:303-7 pubmed
    ..for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years...
  30. Bonifácio C, Cunha C, Muller A, Timóteo C, Dias J, Moura I, et al. Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri. Acta Crystallogr D Biol Crystallogr. 2003;59:345-7 pubmed
    Crystals of cytochrome c peroxidase from Pseudomonas stutzeri were obtained using sodium citrate and PEG 8000 as precipitants. A complete data set was collected to a resolution of 1...
  31. Bidwai A, Witt M, Foshay M, Vitello L, Satterlee J, Erman J. Cyanide binding to cytochrome c peroxidase (H52L). Biochemistry. 2003;42:10764-71 pubmed
    Cyanide binding to a cytochrome c peroxidase (CcP) variant in which the distal histidine has been replaced by a leucine residue, CcP(H52L), has been investigated as a function of pH using spectroscopic, equilibrium, and kinetic methods...
  32. Hays Putnam A, Lee Y, Goodin D. Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide. Biochemistry. 2009;48:1-3 pubmed publisher
    A proposed electron transfer pathway in cytochrome c peroxidase was previously excised from the structure by design. The engineered channel mutant was shown to bind peptide surrogates without restoration of cyt c oxidation...
  33. Paes de Sousa P, Pauleta S, Rodrigues D, Simões Gonçalves M, Pettigrew G, Moura I, et al. Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study. J Biol Inorg Chem. 2008;13:779-87 pubmed publisher
    ..This work reports the first electrochemical study of the electron transfer between a bacterial cytochrome c peroxidase and horse heart cytochrome c...
  34. Pettigrew G, Pauleta S, Goodhew C, Cooper A, Nutley M, Jumel K, et al. Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans containing more than one cytochrome. Biochemistry. 2003;42:11968-81 pubmed
    ..F., Cooper, A., Nutley, M., Jumel, K., and Harding, S. E. (2003) Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans, Biochemistry 42, 2046-2055], cytochrome c peroxidase of Paracoccus ..
  35. Timóteo C, Tavares P, Goodhew C, Duarte L, Jumel K, Gírio F, et al. Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri. J Biol Inorg Chem. 2003;8:29-37 pubmed
    The production of cytochrome c peroxidase (CCP) from Pseudomonas ( Ps.) stutzeri (ATCC 11607) was optimized by adjusting the composition of the growth medium and aeration of the culture...
  36. Bateman L, Leger C, Goodin D, Armstrong F. A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction. J Am Chem Soc. 2001;123:9260-3 pubmed
    A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction...
  37. Harvey J, Bathelt C, Mulholland A. QM/MM modeling of compound I active species in cytochrome P450, cytochrome C peroxidase, and ascorbate peroxidase. J Comput Chem. 2006;27:1352-62 pubmed
    ..Two heme peroxidases, Cytochrome c Peroxidase (CcP) and Ascorbate Peroxidase (APX), have a structurally very similar active site, yet have active ..
  38. Meharenna Y, Doukov T, Li H, Soltis S, Poulos T. Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate. Biochemistry. 2010;49:2984-6 pubmed publisher
    ..The 1.40 A crystal structure of cytochrome c peroxidase Compound I has been determined as a function of X-ray dose while the visible spectrum was being monitored...
  39. Hadfield A. Electron-induced enzyme activation. Structure. 2006;14:1-2 pubmed
  40. Kuo C, Fridovich I. Stimulation of the activity of horseradish peroxidase by nitrogenous compounds. J Biol Chem. 1988;263:3811-7 pubmed
    ..The peroxidation of dianisidine catalyzed by cytochrome c peroxidase was affected by the nitrogenous compounds, but to a lesser extent than was the action of HRP...
  41. Nóbrega C, Saraiva I, Carreira C, Devreese B, Matzapetakis M, Pauleta S. The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase. Biochim Biophys Acta. 2016;1857:169-176 pubmed publisher
    ..The heterologously expressed Laz was shown to be a competent electron donor to N. gonorrhoeae cytochrome c peroxidase. This is an evidence for its involvement in the mechanism of protection against hydrogen peroxide ..
  42. Vladimirov Y, Proskurnina E, Izmailov D, Novikov A, Brusnichkin A, Osipov A, et al. Cardiolipin activates cytochrome c peroxidase activity since it facilitates H(2)O(2) access to heme. Biochemistry (Mosc). 2006;71:998-1005 pubmed
    ..These data suggest that cardiolipin activates specifically Cyt c peroxidase activity not only because it promotes Fe...S(Met80) bond breaking but also facilitates H2O2 penetration to the reaction center. ..
  43. Erman J, Vitello L, Pearl N, Jacobson T, Francis M, Alberts E, et al. Binding of Yeast Cytochrome c to Forty-Four Charge-Reversal Mutants of Yeast Cytochrome c Peroxidase: Isothermal Titration Calorimetry. Biochemistry. 2015;54:4845-54 pubmed publisher
    Previously, we constructed, expressed, and purified 46 charge-reversal mutants of yeast cytochrome c peroxidase (CcP) and determined their electronic absorption spectra, their reaction with H2O2, and their steady-state catalytic ..
  44. Minard K, McAlister Henn L. Antioxidant function of cytosolic sources of NADPH in yeast. Free Radic Biol Med. 2001;31:832-43 pubmed
    ..isocitrate dehydrogenase (IDP2)] and in genes encoding two major cellular peroxidases [mitochondrial cytochrome c peroxidase (CCP1) and cytosolic catalase (CTT1)]...
  45. van der Bliek A, Koehler C. A mitochondrial rhomboid protease. Dev Cell. 2003;4:769-70 pubmed
    ..Recent publications demonstrate that yeast mitochondria contain a rhomboid protease required for the cleavage of two mitochondrial intermembrane space proteins, suggesting that rhomboid proteases play a regulatory role in mitochondria. ..
  46. Khademian M, Imlay J. Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor. Proc Natl Acad Sci U S A. 2017;114:E6922-E6931 pubmed publisher
    ..The OxyR response appears to exploit this H2O2 as a terminal oxidant while simultaneously defending the cell against its toxicity. ..
  47. Campos E, Hermes Lima M, Smith J, Prichard R. Characterisation of Fasciola hepatica cytochrome c peroxidase as an enzyme with potential antioxidant activity in vitro. Int J Parasitol. 1999;29:655-62 pubmed
    b>Cytochrome c peroxidase oxidises hydrogen peroxide using cytochrome c as the electron donor. This enzyme is found in yeast and bacteria and has been also described in the trematodes Fasciola hepatica and Schistosoma mansoni...
  48. Pfister T, Gengenbach A, Syn S, Lu Y. The role of redox-active amino acids on compound I stability, substrate oxidation, and protein cross-linking in yeast cytochrome C peroxidase. Biochemistry. 2001;40:14942-51 pubmed
    ..Trp51 and Trp191) and six tyrosines (Tyr36, Tyr39, Tyr42, Tyr187, Tyr229, and Tyr236) in yeast cytochrome c peroxidase (CcP) has been probed by site-directed mutagenesis...
  49. Pappa H, Li H, Sundaramoorthy M, Arciero D, Hooper A, Poulos T. Crystallization and preliminary crystallographic analysis of cytochrome c553 peroxidase from Nitrosomonas europaea. J Struct Biol. 1996;116:429-31 pubmed
    ..A complete data set was obtained to 2.5A and the data were indexed in space group P2(1) with a = 88.79 A, b = 55.93 A, c = 144.37 A, beta = 103.87 degrees. The self-rotation function indicates one homodimer per asymmetric unit. ..
  50. Osipov A, Stepanov G, Vladimirov Y, Kozlov A, Kagan V. Regulation of cytochrome C peroxidase activity by nitric oxide and laser irradiation. Biochemistry (Mosc). 2006;71:1128-32 pubmed
    ..One of the most important events in the development of apoptosis is the enhancement of cytochrome c peroxidase activity upon its interaction with cardiolipin, which modifies the active center of cytochrome c...
  51. Yan X, Xiong K, Luo X, Struble R, Clough R. beta-Secretase expression in normal and functionally deprived rat olfactory bulbs: inverse correlation with oxidative metabolic activity. J Comp Neurol. 2007;501:52-69 pubmed
    ..The results point to a biological role of BACE in synapse function and plasticity as well as a potential mechanism whereby reduced neuronal activity or metabolism could lead to amyloid overproduction in synaptic terminals. ..
  52. Ivancich A, Dorlet P, Goodin D, Un S. Multifrequency high-field EPR study of the tryptophanyl and tyrosyl radical intermediates in wild-type and the W191G mutant of cytochrome c peroxidase. J Am Chem Soc. 2001;123:5050-8 pubmed
    ..EPR) spectroscopy has been used to characterize radical intermediates in wild-type and Trp191Gly mutant cytochrome c peroxidase (CcP)...
  53. Meharenna Y, Oertel P, Bhaskar B, Poulos T. Engineering ascorbate peroxidase activity into cytochrome c peroxidase. Biochemistry. 2008;47:10324-32 pubmed publisher
    b>Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to reducing substrates...