Cytochrome schematic model

Fig. 5-24. Schematic model of sub-unit II of cytochrome oxidase. 1 vo hydrophobic helices anchor the sub-unit to the membrane. The CuA binding site is indicated in a location outside the membrane close to the COOH-terminal end of the peptide. Invariant amino acid residues are shown. Reproduced from Holm et al. (1987).

Figure 3. Schematic model of the sites of oxidation of cytochrome c and guaiacol by cytochrome c peroxidase. Guaiacol migrates down the access channel and reacts with the heme near the 5-meso carbon atom. Styrene also migrates down the channel to react with the ferryl oxygen.

Figure 4. Computer simulation of the interaction between human cytochrome c and cardiolipin tetralinoleoyl (A) and a schematic drawing ( kendama model) of the interaction...

Figure 1 (a) Schematic representation of yeast cytochrome c peroxidase (CcP) structure with heme and key active site residues represented as ball-and-stick models, (b) Active site architecture of yeast cytochrome c peroxidase (CcP) showing the role of all the key residues in catalysis. The dashed lines represent hydrogen bonds... 

A schematic representation of how a decrease in oxygen tension (hypoxia) may affect carotid body glomus cell function. In the mitochondrial model, hypoxia affects either reactive oxygen species (ROS) production or ATP production of mitochondria. Both of these may affect the outward flux of potassium via the potassium channel with the downstream effects shown in the diagram. In the membrane model, the ROS production by membrane-bound molecules (cytochromes) is oxygen sensitive, and thereby affected by hypoxia. Thus, these membrane-bound molecules function as proximal oxygen sensors and cause effects on potassium channels with the downstream effects described in the figure and in the text... 

The schematic shown in Eigure 8.10 is a rather accurate portrayal of the orientation of cytochrome P450 in the ER membrane. Above the ER membrane it can be seen that the heme-containing portion of the GYP is oriented toward the cell cytoplasm, whereas the N-terminal end of the GYP is oriented toward the lumen of the SER. Compare Figure 8.10 with Figure 8.11, which is a homology model of rat cytochrome P450 2B1. Both models depict the major portion of the GYP protein presented to the cell cytoplasm while a helical portion of the protein anchors it to the SER membrane. 

Figure 6-3 Model proposed by Gilmour et al. [17] for the calcium binding mechanism to cytochrome c peroxidase from P. denitrificans (adapted from [17]). P. denitrtficans CCP is schematically represented in the following way the lighter and darker circles correspond to the C-terminal domain (which includes the high-potential center) and the N-terminal domain (which includes the low-potential center) respectively. Two types of calcium binding sites are illustrated as proposed by Gilmour et al. [17]. S, substrate (cytochrome csso).

Fig. 16 Schematic coupling model of the photo-switchable interactions between cytochrome c and the mixed SAM of spiropyran/merocyanine-terminated and 4-pyridine thiol with (a) the reduction of O2 by COx and (c) the oxidation of lactate by lactate dehydrogenase (LDH). (b) When the electrode is in the cationic merocyanine state, repulsive interactions disallow the functioning of the bioelectrocatalytic processes [130].

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