Escherichia coli cytochrome

Allen JW, Leach N, Ferguson SJ (2005) The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus. Biochem J 389 587-592... 

Gwyer, J.D., Richardson, D.J., and Butt, J.N. (2006) Inhibiting Escherichia coli cytochrome c nitrite reductase voltammetry reveals an enzyme equipped for action despite the chemical challenges it may face in vivo. 

Borisov V, Arutyunyan AM et al (1998) Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome Bd with ligands. Biochemistry 38 740-750... 

Although reduction of chromate Cr to Cr has been observed in a number of bacteria, these are not necessarily associated with chromate resistance. For example, reduction of chromate has been observed with cytochrome Cj in Desulfovibrio vulgaris (Lovley and Phillips 1994), soluble chromate reductase has been purified from Pseudomonas putida (Park et al. 2000), and a membrane-bound reductase has been purified from Enterobacter cloacae (Wang et al. 1990). The flavoprotein reductases from Pseudomonas putida (ChrR) and Escherichia coli (YieF) have been purified and can reduce Cr(VI) to Cr(III) (Ackerley et al. 2004). Whereas ChrR generated a semi-quinone and reactive oxygen species, YieR yielded no semiquinone, and is apparently an obligate four-electron reductant. It could therefore present a suitable enzyme for bioremediation. 

Goodacre, R. Karim, A. Kaderbhai, M. A. Kell, D. B. Rapid and quantitative analysis of recombinant protein expression using pyrolysis mass spectrometry and artificial neural networks Application to mammalian cytochrome b5 in Escherichia coli. J. Biotechnol. 1994,34,185-193. 

Uno, T., Nakao, A., Masuda, S. et al. (2006) Modification of small molecules by using cytochrome P450 expressed in Escherichia coli. Journal of Industrial Microbiology Biotechnology, 33, 1043-1050. 

Parikh, A., Gillam, E.M. and Guengerich, F.P. (1997) Drug metabolism by Escherichia coli expressing human cytochromes P450. Nature Biotechnology, 15, 784—788. 

Leonard, E. and Koffas, M.A. (2007) Engineering of artificial plant cytochrome P450 enzymes for synthesis of isoflavones by Escherichia coli. Applied and Environmental Microbiology, 73, 7246—7251. 

HALKIER, B.A., NIELSEN, H.L., KOCH, B., M0LLER, B.L., Purification and characterization of recombinant cytochrome P450TYR expressed at high levels in Escherichia coli, Arch. Biochem. Biophys., 1995,322, 369-377. 

BARNES, H.J., Maximizing expression of eukaryotic cytochromes P450 in Escherichia coli, Meth. Enzymol., 1996, 272, 3-14. 

BARNES, H.J., ARLOTTO, M.P., WATERMAN, M.R., Expression and enzymatic activity of recombinant cytochrome P450 17a-hydroxylase in Escherichia coli, Proc. Natl. Acad. Sci. USA, 1991,88, 5597-5601. 

GILLAM, E.M.J., BABA, T, KIM, B-R., OHMORI, S., GUENGERICH, F.P., Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme, Arch. Biochem. Biophys., 1993, 305, 123-131. 

Although electron transfers in biological systems are generally expected to be non-adiabatic, it is possible for some intramolecular transfers to be close to the adiabatic limit, particularly in proteins where several redox centers are held in a very compact arrangement. This situation is found for example in cytochromes C3 of sulfate-reducing bacteria which contain four hemes in a 13 kDa molecule [10, 11], or in Escherichia coli sulfite reductase where the distance between the siroheme iron and the closest iron of a 4Fe-4S cluster is only 4.4 A [12]. It is interesting to note that a very fast intramolecular transfer rate of about 10 s was inferred from resonance Raman experiments performed in Desulfovibrio vulgaris Miyazaki cytochrome Cj [13]. 

Voordouw G, Pollock WBR, Bruschi M, et al. 1990. Functional expression of Desulfovibrio vulgaris Hildenborough cytochrome Cj in Desulfovibrio desulfuri-cans following conjngational gene transfer from Escherichia coli. J Bacteriol 172 6122-6. 

Cyclic voltammetry has been also used for estimation of the rate constants for oxidation of water-soluble ferrocenes in the presence of HRP (131). There is a perfect match between the data obtained spectrophotometrically and electrochemically (Table IV), which proves that the cyclic voltammetry reveals information on the oxidation of ferrocenes by Compound II. It is interesting to note that an enzyme similar to HRP, viz. cytochrome c peroxidase, which catalyzes the reduction of H202 to water using two equivalents of ferrocytochrome c (133-136), is ca. 100 times more reactive than HRP (131,137). The second-order rate constant equals 1.4 x 106 M-1 s 1 for HOOCFc at pH 6.5 (131). There is no such rate difference in oxidation of [Fe(CN)e]4- by cytochrome c peroxidase and HRP (8). These comparisons should not however create an impression that the enzymatic oxidation of ferrocenes is always fast. The active-R2 subunit of Escherichia coli ribonucleotide reductase, which has dinuclear nonheme iron center in the active site, oxidizes ferrocene carboxylic acid and other water-soluble ferrocenes with a rate constant of... 

Cytochrome b562, Fe11 Escherichia coli 0.25 Haem, N (His), S (Met) 6... 

The cytochrome bS62 from Escherichia coli involves histidine and methionine axial ligands as shown by crystallographic studies.716... 

The cytochrome o from Azotobacter vinelandii is reported to consist of one polypeptide of molecular weight 28 000 with two identical heme components. It has also been isolated from the thermophile PS3,1319 Escherichia coli, Vitreoscilla, Pseudomonas aeruginosa, and Rhodopseudomonas spp. The enzyme from Vitreoscilla consists of two identical polypeptides of molecular weight 13 000 and two moles of protoheme IX. A cytochrome b562-o complex from E. coli contains two peptides and, strangely, copper.1320... 

Hyde, G.E. Campbell, W.H. (1990). High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH-nitrate, reductase and its comparison to human NADH-cytochrome b5 reductase. Biochemical and Biophysical Research Communications 168, 1285-91. 

Shirabe, K., Yubisui, T. Takeshita, M. (1989). Expression of human erythrocyte NADH-cytochrome 65 reductase as a thrombin-cleavable fused protein in Escherichia coli. Biochimica et Biophysica Acta 1008, 189-92. 

McGinnity DF, Griffin SJ, Moody GC, et al. Rapid characterization of the major dmg-metabolizing human hepatic cytochrome P-450 enzymes expressed in Escherichia coli. Dmg Metab Dispos 1999 27 1017-1023. 

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