Glutamic acid cytochrome

Backgren, C., Hummer, G., Wiksstroem, M, and Puustinen, A. (2000) Proton translocation by cytochrome c oxidase can take place without conserved glutamic acid in subunit I., Biochemistry, 39, 7863-7867. 

Wakabayashi, S., Takeda, H., Matsubara, H., Kim, C. H., and King, T. E., 1982, Identity of the heme-not-containing protein in bovine heart cytochrome c, preparation with the protein mediating cl-c complex formationoa protein with high glutamic acid content, J. Biochem. (Tokyo) 91 2077n2085. 

Figure 17 Time-resolved SS-FTIR spectra of photodissociated CO Cytochrome bo-i from E. coli. The inset shows the evolution of the glutamic acid 286 difference feature. The noise level in the spectrum is indicated by the flat region between 1800 and 1900 cm ...

Guengerich FP, Hanna IH, Martin MV, Gillam EM. Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis. Biochemistry 2003 42 1245-53. 

Menaquinone (vitamin K2) mediates electron transfer between dehydrogenases and the cytochromes and is the major electron carrier cofactor during anaerobic growth of E. coli. Vitamin K is also an essential cofactor in the post-translational carboxylation of glutamic acid residues in several protein systems [200]. 

It has been suggested that effects on cerebral enzyme systems other than cytochrome c oxidase may contribute to neurotoxic effects (Petterson and Cohen, 1993). Thus, inhibition of glutamate decarboxylase can result in a depletion of the inhibitory neurotransmitter y-aminobutyric acid (GABA), possibly predisposing to the development of convulsions (Tursky and Sajter, 1962). Persson et al. (1985) found that CN (5-20 mg NaCN kg-1, ip) increased glutamic acid concentrations in the cerebellum,... 

Similar calculations have been Initiated to ascertain the relative midpoints of the two bacterlochlorophylls (Bh and Bl) and the two bacteriopheophytins (Hl and Hm)- The assumptions used were the same as those outlined above for the cytochrome calculations, except that glutamic acid L104 is uncharged. It has been found that this residue can be replaced with non-polar amino acids without loss of function (30). These calculations suggest that the L side is only very slightly easier to reduce than the M branch, the differences between Bl and Bm and between Hl and Hm are less than 60 meV. Similar results were found when the protein was assumed be surrounded by water or by a low dieletric, such as a membrane. RC function with little change in the native membrane, solubilized with detergent or even suspended in hexane (31). 

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