Binding, cytochrome

No region of the cytochrome penetrates the membrane nevertheless, the cytochrome subunit is an integral part of this reaction center complex, held through protein-protein interactions similar to those in soluble globular multisubunit proteins. The protein-protein interactions that bind cytochrome in the reaction center of Rhodopseudomonas viridis are strong enough to survive the purification procedure. However, when the reaction center of Rhodohacter sphaeroides is isolated, the cytochrome is lost, even though the structures of the L, M, and H subunits are very similar in the two species. 

A trianionic zinc porphyrin anchored to a membrane by an imidazole link has been used to bind cytochrome c at the membrane surface. UV spectra confirmed the insertion of the zinc porphyrin into the phospholipid vesicle and was used to study surface association of cytochrome c. 

Fig. 2 Molecular wires that bind cytochrome P450CAM...

Hydrogen cyanide binds cytochrome oxidase, resulting in cellular hypoxia and rapid death. 

The formation of a reversible Michaelis-Menten-type complex of the enzyme and ferrocytochrome c [ES1S2 in Eq. (3) ] can be postulated from initial steady-state kinetics of the cytochrome c peroxidase reaction (17). Since cytochrome c peroxidase and cytochrome c are acidic and basic proteins, respectively, their interaction may be governed principally by electrostatic attraction. This assumption is further supported by the fact that several polycations which reversibly and irreversibly bind cytochrome c peroxidase inhibit its enzymic activity in competition with ferrocytochrome c 17,62). 

The flavocytochrome b2 molecular surface which is buried and hidden from solvent on binding cytochrome c has a total area of 657. The model... 

Milieu, F., De Jong, C., Paulson, L., Capaldi, R. A., Identiflcation of Specific Carboxylate Groups on Cytochrome C Oxidase That Are Involved in Binding Cytochrome C , Biochemistry (Wash.) 22 (1983) 546-552. 

It can be concluded that CH6 as well as other aptamers bind cytochrome c rather unspeciflcally by ionic interactions of the polyanionic DNA and a protein containing a cationic cluster, at least when the aptamers are immobilized, as in SPR experiments. 

Figure 19 A 4,4 -disubstituted Ru(II) fns-bipyridine core (17) used to project protein-binding recognition elements. The Wilson group has used the core along with an aspartate taminated substituent (18) and Kato et al. have used the core along with a phenylalanine terminated substituent (19) to bind cytochrome c and a-chymotrypsin, respectively.

Fig. 135.3 Carotenoid biosynthesis. CHBl carotenoid P-hydroxylase nonheme di-iron monooxygenase, CHB2 carotenoid P-hydroxylase heme-binding cytochrome P450, CHE carotenoid s-hydroxylase heme-binding cytochrome P450 [9,14]...

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