electron-transfer mediator in bacterial respiratory chain

This deposit represents the soluble fragment containing the
functional domain which starts at position 78 and is preceded
by an additional Met residue

The ambiguity code for geminal methylene and methyl protons has been set
to 1 for stereospecific assignments and to 2 for non-stereospecific
assignments. The ambiguity code 9 denotes tentative assignments.

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jul 18 13:17:06 2011

3,3'-(7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-diyl)dipropanoic acid

3-[(5Z,10Z,14Z,19Z)-18-(2-carboxyethyl)-8,13-bis(ethenyl)-3,7,12,17-tetramethyl-21,23-dihydroporphyrin-2-yl]propanoic acid

Pristovsek, P., Luecke, C., Reincke, B., Lohr, F., Ludwig, B., and Rueterjans, H.,
"Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Functional
Domain of Paracoccus denitrificans Cytochrome c552 in the Reduced state,"
J. Biomol. NMR 16, 353-354 (2000).

Complete 1H, 15N and 13C assignment of the functional domain of paracoccus denitrificans cytochrome c552 in the reduced state.

A membrane-bound c-type cytochrome, c552, acts as the electron mediator between
the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory
chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a
soluble cytochrome c interacts with both complexes, the bacterial c552, the
product of the cycM gene, shows a tripartite structure, with an N-terminal
membrane anchor separated from a typical class I cytochrome domain by a highly
charged region. Two derivative fragments, lacking either only the membrane
spanning region or both N-terminal domains, were constructed on the genetic
level, and expressed in Escherichia coli cotransformed with the ccm gene
cluster encoding host-specific cytochrome c maturation factors. High levels of
cytochromes c were expressed and located in the periplasm as holo-proteins;
both these purified c552 fragments are functional in electron transport to
oxidase, as ascertained by kinetic measurements, and will prove useful for
future structural studies of complex formation by NMR and X-ray diffraction.

Reincke, B., Thony-Meyer, L., Dannehl, C., Odenwald,
A., Aidim, M., Witt, H., Ruterjans, H. & Ludwig, B. (1999) Heterologous
expression of soluble fragments of cytochrome c552 acting as electron donor to
the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta,
1441, 114-120.

Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.

Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes
in different branches of their electron transport system. Among the many
cytochromes c present in the soil bacterium Paracoccus denitrificans, a
membrane-bound cytochrome (c552) has been suggested to mediate the electron
transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry,
E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have
purified this cytochrome from cytoplasmic membranes, and cloned and sequenced
its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is
highly similar to type-I cytochromes c, its N-terminal part contains a
hydrophobic segment providing membrane attachment. In addition, we present
immunological evidence for its functional role in respiration.

Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification
of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.
Eur. J. Biochem., 231, 259-265.

Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.

Paracoccus denitrificans cytochrome c552, soluble fragment

Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Reduced State

Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Oxidized State

Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Reduced State

Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Oxidised State

Structure Of The Soluble Domain Of Cytochrome C552 With Its Flexible Linker Segment From Paracoccus Denitrificans

cytochrome C552 [Paracoccus denitrificans]

cytochrome c, class I [Paracoccus denitrificans PD1222]

RecName: Full=Cytochrome c-552; AltName: Full=Cytochrome c552

Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus
denitrificans cytochrome c552 in the reduced state

chemical shift assignments for the oxidized cytochrome c552

relaxation data of reduced cytochrome c552

relaxation data of oxidized cytochrome c552

related BMRB entries (relaxation data) added

small excess sodium dithionite as reducing agent