1.11.1.5: cytochrome-c peroxidase

This is an abbreviated version!
For detailed information about cytochrome-c peroxidase, go to the full flat file.

Word Map on EC 1.11.1.5

Reaction

2 ferrocytochrome c +

H2O2
=
2 ferricytochrome c
+ 2 H2O

Synonyms

apocytochrome c peroxidase, BCcP, CCP, CCP1, CcpA, Cjj0382, CytC, cytochrome c iso-1, cytochrome c peroxidase, cytochrome c-551 peroxidase, cytochrome c-H2O oxidoreductase, cytochrome peroxidase, di-heme cytochrome c peroxidase, diheme cytochrome c peroxidase, diheme cytochrome c5 peroxidase CcpA, DocA, LmP, MacA, mesocytochrome c peroxidase azide, mesocytochrome c peroxidase cyanate, mesocytochrome c peroxidase cyanide, peroxidase, cytochrome c, Psa CcP

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.5 cytochrome-c peroxidase

Crystallization

Crystallization on EC 1.11.1.5 - cytochrome-c peroxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant Strep-tagged mutant enzyme H93G, and wild-type enzyme in reduced, oxidized, and semireduced states, sitting drop vapor diffusion method, 0.001 ml of 7.5 mg/ml protein is mixed with 0.001 ml of reservoir solution containing for the oxidized enzyme 0.1 M ammonium acetate buffer, pH 5.5, 1.3 M Na/K phosphate and 6% v/v of ethanol, for the ascorbate reduced enzyme 0.1 M HEPES/NaOH buffer, pH 7.5, 0.2 M ammonium acetate, and 25% w/v PEG 3350, and for the dithionite reduced enzyme 0.1 M sodium citrate buffer, pH 5.6, and 1 M ammonium phosphate, mutant MacA_H93G crystals are obtained in 1 M ammonium sulfate, pH 5.4, X-ray diffraction structure determination and analysis at 1.2-2.3 A resolution
sitting-drop vapor diffusion, 16% PEG 10000, 0.1 HEPES/NaOH, pH 7.4, 293K, wild-type enzyme, space group P1, 2.00 A resolution, mutant enzyme G94K/K97Q/R100I, space group P4321, 3.21 A resolution, mutant enzyme S134P/V135K, space group P21, 2.40 A resolution, mutant enzame S134P, space group P21, 2.40 A resolution
enzyme in complex with wild-type cytochrome c or cytochrome c mutant DELTA10LmCytc, hanging-drop vapour diffusion method, protein in 40 mM potassium phosphate, pH 6.5, 32-33% pentaerythritol ethoxylate and 4% acetone as precipitant, X-ray diffraction structure determination and analysis at 1.84-2.29 A resolution
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the enzyme crystallizes in two different forms obtained at pH 4 and pH 5.3, corresponding to form IN, inactive, and OUT, active. In the form OUT, the calcium binding site is fully occupied by Ca2+, coordinated by seven ligands in a distorted pentagonal bipyramidal geometry, and four water molecules
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resolution 1.8 A
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hanging-drop vapour-diffusion method
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structures of the inactive oxidized and active mixed valence enzyme, model of the activation process
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of mutant D37E/V45E/H181E in a metal-free form and with Co2+ at the designed Mn2+ site, mutant is a close structural model of the Mn2+ binding site in manganese peroxidase
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diffraction limit 2.5 A
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resolution 2.4 A
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with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol
under cryogenic conditions using synchrotron radiation
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fully oxidized form, reveals that a segment of 10 amino acids near the peroxide binding site is disordered in all four molecules of the asymmetric unit of the crystal. Flexibility in this part of the molecular scaffold correlates with the levels of activity seen in cytochrome c peroxidases characterized so far
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hanging-drop vapour-diffusion method
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apo and holo CcP exhibit very similar structural, hydrodynamic, and thermodynamic properties. Apo CcP is more expanded in solution, displays a number of characteristics associated with a molten globule state, and does not form an unfolding intermediate during thermal and chemical denaturation
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apo- and holoenzyme
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crystal structure
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microdialysis, in 500 mM potassium phosphate, pH 6.0, against 50 mM potassium phosphate, pH 6.0, containing 30% 2-methyl-2,4-pentanediol
modified enzyme
of iron-free enzyme, removal of iron has no effect on porphyrin geometry and distortion, indicating that iron coordination is not responsible for prophyrin conformation. Iron depletion leads to changes in solvent structure in the distal pocket which result in changes in the distal H52 acid-base catalyst
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protein channel mutant with surrogate protein (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), vapor diffusion, 200 mM KPi, 25% MPD, pH 6.0, temperature 282K, space group P212121, resolution 1.6 A
structure of fluoride-inhibited enzyme
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structure of NO-inhibited enzyme
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structures for mutants N184R, Y36A, W191F, N184R/W191F, Y36A/W191, FY36A/N184R, Y36A/N184R/W191F, Y36A/N184R/W191F-ascorbate complex, no major perturbations compared to the wild type protein
with comercial kit
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apo- and holoenzyme
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purified recombinnat His-tagged CcpA, sitting drop vapor diffusion, mixing of 0.001 ml 7.5 mg/ml dithionite-reduced protein solution with 0.001 ml of reservoir solution containing 26% w/v PEG 2000 monomethyl ether and 0.1 M bis-(2-hydroxyethyl)-amino-tris-(hydroxymethyl)methane, pH 5.0, equilibration against 0.2 ml of reserrvoir solution, 10% v/v (2R,3R)-butanediol as a cryoprotectant, X-ray diffraction structure determination and analysis
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