Cytochrome c modifiers

F. Lisdat, B. Ge, E. Ehrentreich-Forster, R. Reszka, and F.W. Scheller, Superoxide dismutase activity measurement using cytochrome c-modified electrode. Anal. Chem. 71,1359—1365 (1999). 

K.V. Gobi and F. Mizutani, Efficient mediatorless superoxide sensors using cytochrome c-modified electrodes. Surface nano-organization for selectivity and controlled peroxidase activity. J. Electroanal. Chem. 484, 172-181 (2000). 

K.V. Gobi, Y. Sato, and F. Mizutani, Mediatorless superoxide dismutase sensors using cytochrome c-modified electrodes xanthine oxidase incorporated polyion complex membrane for enhanced activity and in-vivo analysis. Electroanalysis 13, 397-403 (2001). 

NADPH-dependent oxidase in osteoclasts 02 Cytochrome c-modified Au UME (amperometric) [54]... 

Tsou CL (1951) Cytochrome c modified by digestion with proteolytic enzymes. Biochem J 49 362-367... 

NADPH-dependent oxidase in osteoclasts or Au/cytochrome c modified, amperometric 19... 

Not all data in the literature are consistent with ET rates scaling with re- Cytochrome C551 has been ruthenated at His-47 the Ru(II)-to-Fe(III) ET rate is 13 for re = 7.9 A. The driving force for ET is the same as for horse heart cytochrome c modified at His-33, and yet ET is slower (13 vs. 30 s ) for an r that is 3.8 A shorter (146). Several other unusually slow rates for short edge-edge separation distances have been observed for ruthenium-modified blue copper and iron-sulfur proteins (see below). 

The rate of enzyme turnover is usually determined, not simply by the duration of the substrate-product transformation at the enzyme active center, but by the rate of protein globule relaxation. There is much experimental evidence for this statement. For example, a kinetic and structural study of cytochrome C modified by the ruthenium label specifically at the imidazole moiety of histidine 33, demonstrated that the rate of intramolecular electron transfer, Ru(2) - Haem(3), k 55 s" [56], is on the same time scale as the rate of conformational changes occurring within the cytochrome C molecule [57, 58]. Together with other experimental results (see, for references [38, 39]), this is an obvious indication of the protein conformational changes as the rate-limiting step in protein functioning. 

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