Why do c‐type cytochromes exist?

@article{Wood1983WhyDC,
  title={Why do c‐type cytochromes exist?},
  author={P. Wood},
  journal={FEBS Letters},
  year={1983},
  volume={164}
}
  • P. Wood
  • Published 1983
  • Biology, Medicine
  • FEBS Letters
The hypothesis presented is that the different classes of c‐type cytochrome originated as proteins located in the bacterial periplasmic space, or on the periplasmic side of the cytoplasmic membrane. In these locations, covalent bonds between haem and protein prevented the haem from being lost to the surrounding medium. Subsequent evolution has led to internal location of c‐type cytochromes in eucaryotes and cyanobacteria. The covalent links have been retained because of their structural role; a… Expand
Why do c-type cytochromes exist? Reprise.
  • P. Wood
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1991
TLDR
This paper discusses covalent links that characterize c-type haem in relation to Gram-negative and Gram-positive bacteria, cyanobacterial thylakoids and eukaryotes, and analogies are drawn with flavin and pyrroloquinoline quinone as prosthetic groups. Expand
C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems.
TLDR
The progress that has been made in understanding the need for covalent attachment of haem to proteins in cytochromes c and the complex systems involved in their formation are reviewed. Expand
Cytochrome c biogenesis in bacteria
TLDR
NMR studies on this material are consistent with a single and 'normal' attachment of the haem to the polypeptide, which implies that haem provision for cytochrome b 562 synthesis occurs independently of the ccm system. Expand
Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri determined at 2.2A resolution.
TLDR
The structure of the dihaem cytochrome c4, in conjunction with sequence alignment, suggests that the cytochromes c4 protein has evolved by duplication of a cy tochrome c gene. Expand
The Function of Bacterial and Photosynthetic Cytochromes c
This chapter seeks to place our extensive knowledge of the structure and properties of bacterial cytochromes c within the context of the energy-conserving electron transport systems of which they areExpand
A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding
TLDR
A novel octa‐haem c protein, MccA, is described that contains only seven conventional haem c‐binding motifs (CXXCH), in addition to several single cysteine residues and a conserved CH signature. Expand
A novel pathway for cytochromes c biogenesis in chloroplasts.
TLDR
Genetic analyses have identified proteins that are required for the assembly of c-type cytochromes in mitochondria, bacteria and chloroplasts and proposed tryptophan-rich motif, which has been proposed to represent a heme binding site in bacterial cytochrome biogenesis proteins (CcmC and CcmF), is functionally important in plastid CcsA. Expand
The biosynthesis of bacterial and plastidic c-type cytochromes
TLDR
Genetic analysis suggests that the nuclear as well as the plastid genomes encode functions required for heme attachment, and that these genes function in the biosynthesis of the membrane-associated aswell as the soluble c-type cytochrome of chloroplasts. Expand
A brief survey of the "cytochromome".
TLDR
The contribution of multihaem cytochromes c to dissimilatory pathways handling metallic minerals, nitrogen compounds, sulfur compounds, organic compounds and phototrophism are described to set the stage for the further exploration of the vast unknown "cytochromome" that can be anticipated from genomic databases. Expand
Synthesis of holo Paracoccus denitrificans cytochrome c 550 requires targeting to the periplasm whereas that of holo Hydrogenobacter thermophilus cytochrome c 552 does not
Expression from a plasmid of the complete gene, including the codons for the N‐terminal periplasmic targeting signal, for cytochrome c 550 of Paracoccus denitrificans led to the formation of the holoExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 40 REFERENCES
Asymmetry of an energy transducing membrane the location of cytochrome c2 in Rhodopseudomonas spheroides and Rhodopseudomonas capsulata.
TLDR
The cytochromes produced during aerobic growth were immunologically indistinguishable from those produced during photosynthesis, and the implications of these results to energy coupling in the photosynthetic bacteria are discussed. Expand
Periplasmic CO‐binding C‐type cytochrome in a marine bacterium
TLDR
The cell wall layers may be selectively stripped from this ’ bacterium by suitable washing procedures and it therefore offers a unique opportunity to study cytochrome distribution in the cell envelope of Gram-negative bacteria. Expand
Periplasmic location of the terminal reductase in nitrite respiration
  • P. Wood
  • Chemistry, Medicine
  • FEBS letters
  • 1978
TLDR
The dissimilatory nitrite reductase of denitrifying bacteria is a readily solubilised protein which in many cases is released by sonication or French press treatment, and its primary role would seem to be nitrite reduction. Expand
Synthesis, assembly, and localization of periplasmic cytochrome c.
  • W. Garrard
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1972
TLDR
It is concluded that the periplasmic hemoprotein is not a precursor to, or a product of, a membrane-bound or soluble cytoplasmic pigment, and results suggest that c-type cytochromes in this microorganism are assembled from an iron-tetrapyrrole precursor pool. Expand
Interaction of Pseudomonas cytochrome cd1 with the cytoplasmic membrane.
TLDR
A new assay of respiratory nitrite reductase was developed based on determination of the stoichiometrical proton consumption accompanying nitrite reduction, which shows that while the kinetic pattern and the temperature dependence of the activity remain almost the same the molecular activity is enhanced when the enzyme is released from cells. Expand
Structure of the covalently bound flavin of Chlorobium cytochrome.
TLDR
The flavin structure of Chlorobium cytochrome c 553 is 8α-S- cysteinyl-FAD thioether, which confirms the hypothesis that the flavin is covalently linked to the polypeptide chain. Expand
On the evolutionary relationship of the 4-alpha-helical heme proteins. The comparison of cytochrome b562 and cytochrome c'.
TLDR
Structural evidence suggests that the two cytochrome families may have diverged from a common molecular ancestor. Expand
Localization of dehydrogenases, reductases, and electron transfer components in the sulfate-reducing bacterium Desulfovibrio gigas
Various dehydrogenases, reductases, and electron transfer proteins involved in respiratory sulfate reduction by Desulfovibrio gigas have been localized with respect to the periplasmic space,Expand
Studies on the biosynthesis of cytochrome c.
TLDR
The high specific radioactivity of the cytochrome haem indicates that synthesis of the holoenzyme must proceed by direct attachment of haem to the apoprotein rather than by the intermediate formation of a protoporphyrinogen-apoprotein complex. Expand
Pseudomonas cytochrome c peroxidase XI. Kinetics of the peroxidatic oxidation of Pseudomonas respiratory chain components.
  • M. Rönnberg, N. Ellfolk
  • Chemistry, Medicine
  • Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry
  • 1975
TLDR
From the initial velocity patterns a sequential mechanism with compulsory substrate-binding order is proposed for PaCCP, and a comparative kinetic study of the peroxidatic oxidation of cytochrome c-551 by yeast cytochromes c was made to evaluate the significance of electrostatic interactions in complex formation between the enzyme and substrates. Expand
...
1
2
3
4
...