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Cytochrome rc(552), formed during expression of the truncated, thermus thermophilus cytochrome c(552) gene in the cytoplasm of escherichia coli, reacts spontaneously to form protein-bound 2-formyl-4-vinyl (spirographis) heme

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Overview

authors

  • Fee, James
  • Todaro, T. R.
  • Luna, E.
  • Sanders, D.
  • Hunsicker-Wang, L. M.
  • Patel, K. M.
  • Bren, K. L.
  • Gomez-Moran, E.
  • Hill, M. G.
  • Ai, J. Y.
  • Loehr, T. M.
  • Oertling, W. A.
  • Williams, P. A.
  • Stout, C. David
  • McRee, D.
  • Pastuszyn, A.

publication date

  • 2004

journal

  • Biochemistry  Journal

abstract

  • Expression of the truncated (lacking an N-terminal signal sequence) structural gene of Thermus thermophilus cytochrome c(552) in the cytoplasm of Escherichia coli yields both dimeric (rC(557)) and monomeric (rC(552)) 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 rC(557) is comprised of a dimer and has been structurally characterized [McRee, D., et al. (2001) J. Biol. Chem. 276, 6537-6544]. Unexpectedly, the monomeric rC(552) transforms spontaneously to a cytochrome-like chromophore having, in its reduced state, the Q(oo) transition (alpha-band) at 572 nm (therefore called p572). The X-ray crystallographic structure of rC(552), at 1.41 A resolution, shows that the 2-vinyl group of heme ring I is converted to a [heme-CO-CH(2)-S-CH(2)-C(alpha)] conjugate with cysteine 11. Electron density maps obtained from isomorphous crystals of p572 at 1.61 A resolution reveal that the 2-vinyl group has been oxidized to a formyl group. This explains the lower energy of the Q(oo)() 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 (1)H 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.

subject areas

  • Circular Dichroism
  • Crystallography, X-Ray
  • Cytochrome b Group
  • Cytochrome c Group
  • Cytoplasm
  • Electron Transport
  • Electron Transport Complex IV
  • Escherichia coli
  • Heme
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Models, Molecular
  • Molecular Structure
  • Oxidation-Reduction
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Deletion
  • Spectrum Analysis
  • Spectrum Analysis, Raman
  • Thermus thermophilus
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi0489681

PubMed ID

  • 15379555
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Additional Document Info

start page

  • 12162

end page

  • 12176

volume

  • 43

issue

  • 38

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