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Cytisine binding affinities of in the pyridyl ether series. Data from refs. 7 and 11

Cytoarchitecture of medial prefrontal cortex. A. Photomicrograph reveal the pattern of AChE and Nissl staining, respectively. Arrowheads indicate boundaries of cortical regions delineated by AChE and Nissl staining. Structures between the arrowheads from dorsal to ventral are

Cytoarchitecture of olfactory cortex. A-H. Nissl stained coronal sections through olfactory related structures, principally showing the piriform and entorhinal cortices and amygdala nuclei. Bar in H, 1 mm.

Cytoarchitecture of the AON. A-D. Nissl stained coronal sections through different rostral to caudal levels of AON. Bar in D, 1 mm.

Cytoarchitecture of the main olfactory bulb. Coronal section of the olfactory bulb stained with cresyl violet at low magnification in A and higher magnification in B. Bar in A, 1 mm.

Cytochalasin D

Cytochrome 6 turnover .

Cytochrome bci inhibitor structures.

Cytochrome BF Contribution to Proton Gradient. The cytochrome bf complex oxidizes QH2 to Q

Cytochrome bf contribution to proton gradient. The cytochrome bf complex oxidizes QH2 to Q through the Q cycle. Four protons are released into the thylakoid lumen In each cycle.

Cytochrome bS59 photooxidation in spinach chioropiasts Photoreduction of cytochrome b5S9 in a photosystem-ll subchloroplast particle. Biochim Biophys Acta 256

Cytochrome c and its relationship to the inner mitochondrial membrane.

Cytochrome c as an example of a small metal-rich protein, backbone schematic, viewed as in a. The backbone forms an approximate up and down cylinder with the heme tucked into the center, but the elements forming the cylinder are a mixture of helices and extended strands.

Cytochrome c oxidase a general

Cytochrome c oxidase model complexes, , as synthesized in reference 149.

Cytochrome c oxidase structure structure of the redox centers. Hemes and copper ions are colored as above. Oxygen

Cytochrome c oxidase the anionic 1

Cytochrome c reduction by 02 Production of 02 from activated neutrophils may be assayed using cytochrome c. Oxidised has a higher affinity for 02 than does cytochrome c thus, the addition of SOD to activated neutrophil suspensions will prevent the reduction of cytochrome c. SOD-inhibitable cytochrome c reduction is therefore a direct measure of the rate of 02 formation.

Cytochrome c. The heme is linked to the protein by four bonds. Two bonds are from two protein cysteine-S atoms to the No. 2 and No. 4 side chains of the heme. The other two bonds are from two N atoms of the protein to the central iron atom, one N atom being below the plane of the porphyrin ring and another N atom being above the plane of the ring.

Cytochrome c3 amino add sequences. Amino acid sequences are given for Miyazaki . Numbering is for Miyazaki cytochrome c3. Heme labeling is consistent with assignments from the Miyazaki cytochrome c3 three-dimensional structure

Cytochrome c554 isolated from Nitrosomonas europaea

Cytochrome c554 isolated from Nitrosomonas europaea PDB code

Cytochrome C556 fragment Pep18 with a datively anchored diiron hexacarbonyl cluster and a photosensitizing Ru polypyridine complex .

Cytochrome model complexes

Cytochrome oxidase mechanism. The cycle begins and ends with all prosthetic groups in their oxidized forms . Reduced forms are in red. Four cytochrome c molecules donate four electrons, which, in allowing the binding and cleavage of an molecule, also makes possible the import of four from the matrix to form two molecules of H2O. which are released from the enzyme to regenerate the initial state.



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