Cytochrome chemically modified

Garcia-Arellano, H. Valderrama, B. Saab-Rincon, G., and Vazquez-Duhalt, R., High Temperature Biocatalysis by Chemically Modified Cytochrome c. Bioconjugate Chem. 2002. 13 pp. 1336-1344. 

Garcia-Arellano, H. Buenrostro-Gonzalez, E. and Vazquez-Duhalt, R., Biocatalytic transformation of petroporphyrins by chemical modified cytochrome, C. Biotechnology and Bioengineering, 2004. 85(7) pp. 790-798. 

Reaction with Chemically Modified Cytochrome c. Chemically modified (CDNP) cytochrome c derivatives have been prepared by Margoliash and colleagues (22). Lysine residues react as in (17),... 

Garcia-Arellano H, Valderrama B, Saab-Rincon G et al (2002) High temperature biocatalysis by chemically modified cytochrome c. Bioconjug Chem 13 1336-1344... 

However, cytochrome a has no oxidase activity in cooperation with chemically modified cytochrome c which is capable of reducing cytochrome a at almost the maximal rate, if a generating system for... 

The Effect of Chemically Modified Cytochrome c on Cytochrome Oxidase Activity Takemori et al., 1962)... 

To study the formation of a complex between cytochromes a and c, chemically modified cytochrome c was used in experiments on the cytochrome oxidase activity in place of native cytochrome c. As is known well, about twenty lysine residues are present per molecule of cytochrome c. About 70% of these were acetylated with acetic anhydride (Section II.B.2.a). In other experiments, about 70% of these groups were succinylated with succinic anhydride (Section II.B.2.6). By these procedures, it is generally believed that the e-NHj group of lysine is substituted first, although there is some possibility that in the above treatment not only this group but also the other amino acid residues such as histidine are substituted. 

Fig. 15. Effect of chemically modified cytochrome c on the reduction of cytochrome a. (A) Acetylated cytochrome c. (B) Succinylated cytochrome c. The sample cuvette contained 9.1 x 10" M phosphate buffer at pH 7.4, 1% Emasol 1130, 3.3 X I0 MKCN, 2.5 x I O M cytochrome a, 1.0 x 10 M hydroqui-none, and 4.5 x I0" M cytochrome c or 4.8 x 10 M modified cytochrome c. The total volume was 3.0 ml. The reaction was initiated by the addition of hydro-quinone. The reduction was determined by measuring the increase in optical density of the

Fig. 16. Effect of chemically modified cytochrome c on the cytochrome oxidase activity of cytochrome a. The activity was measured manometrically as described in the previous communication (Yonetani, 1959). Key (A) native cytochrome c (B) 22% succinylated cytochrome c or 32% acetylated cytochrome c.

Electron-transfer (ET) reactions, the simplest chemical transformations, play vital roles in a diverse ensemble of biological processes. Biological electron transfer is an extraordinarily vibrant field of inquiry, responsible for thousands of original research articles during the past decade. This chapter will focus on studies of ET in chemically modified proteins, protein-protein complexes, and two key biological energy transduction pathways, photosynthesis (see Photosynthesis) and respiration (see Cytochrome Oxidase). 

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