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- W2073126302 abstract "Expression of the truncated (lacking an N-terminal signal sequence) structural gene of Thermus thermophilus cytochrome c552 in the cytoplasm of Escherichia coli yields both dimeric (rC557) and monomeric (rC552) cytochrome c-like proteins [Keightley, J. A., et al. (1998) J. Biol. Chem. 273, 12006−12016], which form spontaneously without the involvement of cytochrome c maturation factors. Cytochrome rC557 is comprised of a dimer and has been structurally characterized [McRee, D., et al. (2001) J. Biol. Chem. 276, 6537−6544]. Unexpectedly, the monomeric rC552 transforms spontaneously to a cytochrome-like chromophore having, in its reduced state, the Qoo transition (α-band) at 572 nm (therefore called p572). The X-ray crystallographic structure of rC552, at 1.41 Å resolution, shows that the 2-vinyl group of heme ring I is converted to a [heme-CO-CH2-S-CH2-Cα] conjugate with cysteine 11. Electron density maps obtained from isomorphous crystals of p572 at 1.61 Å resolution reveal that the 2-vinyl group has been oxidized to a formyl group. This explains the lower energy of the Qoo transition, the presence of a new, high-frequency band in the resonance Raman spectra at 1666 cm-1 for oxidized and at 1646 cm-1 for reduced samples, and the greatly altered, paramagnetically shifted 1H NMR spectrum observed for this species. The overall process defines a novel mechanism for oxidation of the 2-vinyl group to a 2-formyl group and adds to the surprising array of chemical reactions that occur in the interaction of heme with the CXXCH sequence motif in apocytochromes c." @default.
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- W2073126302 date "2004-09-01" @default.
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- W2073126302 title "Cytochrome <i>rC</i><sub>552</sub>, Formed during Expression of the Truncated, <i>Thermus thermophilus</i> Cytochrome <i>c</i><sub>552</sub> Gene in the Cytoplasm of <i>Escherichia coli</i>, Reacts Spontaneously To Form Protein-Bound 2-Formyl-4-vinyl (<i>Spirographis</i>) Heme<sup>,</sup>" @default.
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- W2073126302 doi "https://doi.org/10.1021/bi048968l" @default.
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