EC Number   |
|---|
   1.11.1.5 | 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 |
| 1.11.1.5 | apo- and holoenzyme |
| 1.11.1.5 | crystal structure |
| 1.11.1.5 | diffraction limit 2.5 A |
| 1.11.1.5 | 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 |
| 1.11.1.5 | 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 |
| 1.11.1.5 | hanging-drop vapour-diffusion method |
| 1.11.1.5 | microdialysis, in 500 mM potassium phosphate, pH 6.0, against 50 mM potassium phosphate, pH 6.0, containing 30% 2-methyl-2,4-pentanediol |
| 1.11.1.5 | modified enzyme |
| 1.11.1.5 | 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 |
