The diel activity pattern of mountain hare () on managed heather moorland in Scotland.

The research presented in this paper provides an insight into the behavioral ecology of mountain hares on heather moorland in the Lammermuir Hills of southeast Scotland. We examine the seasonal and diel activity patterns using camera traps over a period of 12 months. The rate of camera detections was calculated for the different divisions of the 24-hr cycle (daylight, dusk, night, and dawn).

Experiences with audio feedback in a veterinary curriculum.

On a national scale in the United Kingdom, student surveys have served to highlight areas within higher education that are not achieving high student satisfaction. Of particular concern to the veterinary and medical disciplines are the persistently poor levels of student satisfaction with academic feedback compared to students in other subjects. In this study we describe experiences with audio feedback trials in a veterinary curriculum.

Peer generation of multiple-choice questions: student engagement and experiences.

A free online system for generation of multiple-choice questions (PeerWise) was implemented in three courses (course A, B, and C) in two different years (second and third year) of a veterinary degree program. Students were asked to author questions, and answer and rate each other's questions. Student experiences of the system were explored using an online survey.

Artefacts induced on c-type haem proteins by electrode surfaces.

In this work it is demonstrated that the characterization of c-type haem containing proteins by electrochemical techniques needs to be cautiously performed when using pyrolytic graphite electrodes. An altered form of the cytochromes, which has a redox potential 300 mV lower than that of the native state and displays peroxidatic activity, can be induced by interaction with the pyrolytic graphite electrode. Proper control experiments need to be performed, as altered conformations of the enzymes containing c-type haems can show activity towards the enzyme substrate.

Pressure perturbation calorimetry and the thermodynamics of noncovalent interactions in water: comparison of protein-protein, protein-ligand, and cyclodextrin-adamantane complexes.

Pressure perturbation calorimetry measurements on a range of cyclodextrin-adamantane, protein-ligand (lysozyme-(GlcNac)(3) and ribonuclease-2'CMP) and protein-protein (cytochrome c peroxidase-pseudoazurin) complexes in aqueous solution show consistent reductions in thermal expansibilities compared to the uncomplexed molecules. Thermodynamic data for binding, obtained by titration calorimetry, are also reported. Changes in molar expansibilities can be related to the decrease in solvation during complexation.

Calcium-dependent heme structure in the reduced forms of the bacterial cytochrome c peroxidase from Paracoccus pantotrophus.

This work reports for the first time a resonance Raman study of the mixed-valence and fully reduced forms of Paracoccus pantotrophus bacterial cytochrome c peroxidase. The spectra of the active mixed-valence enzyme show changes in the structure of the ferric peroxidatic heme compared to the fully oxidized enzyme; these differences are observed upon reduction of the electron-transferring heme and upon full occupancy of the calcium site. For the mixed-valence form in the absence of Ca(2+), the peroxidatic heme is six-coordinate and low-spin on the basis of the frequencies of the structure-sensitive Raman lines: the enzyme is inactive.

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.

The bacterial cytochrome c peroxidases contain an electron-transferring haem c (E) and a peroxidatic haem c (P). Many are isolated in an inactive oxidised state. Reduction of the E haem promotes Ca(2+)-dependent spin state and coordination changes at the P haem rendering it accessible to ligand.

Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus.

Bacterial cytochrome c peroxidases contain an electron transferring (E) heme domain and a peroxidatic (P) heme domain. All but one of these enzymes are isolated in an inactive oxidized state and require reduction of the E heme by a small redox donor protein in order to activate the P heme. Here we present the structures of the inactive oxidized and active mixed valence enzyme from Paracoccus pantotrophus.

A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase.

Pseudoazurin binds at a single site on cytochrome c peroxidase from Paracoccus pantotrophus with a K(d) of 16.4 microM at 25 degrees C, pH 6.0, in an endothermic reaction that is driven by a large entropy change.

Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase.

The gene for pseudoazurin was isolated from Paracoccus pantotrophus LMD 52.44 and expressed in a heterologous system with a yield of 54.3 mg of pure protein per liter of culture.

Crystallization and preliminary X-ray diffraction analysis of a dihaem cytochrome c peroxidase from Paracoccus denitrificans.

Cytochrome c peroxidase was isolated from Paracoccus denitrificans and purified to homogeneity in three steps prior to crystallization. Two different diffraction-quality crystal forms were obtained by the hanging-drop vapour-diffusion method using a number of screening conditions. The best (needle-shaped) crystal form is suitable for structural studies and was grown from solutions containing 20% PEG 8000, 0.

Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans containing more than one cytochrome.

According to the model proposed in previous papers [Pettigrew, G. W., Prazeres, S.

The electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans.

We have used microcalorimetry and analytical ultracentrifugation to test the model proposed in Pettigrew et al. [(1999) J. Biol.

Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri.

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. The protein was isolated and characterized biochemically and spectroscopically in the oxidized and mixed valence forms.