| Haem type | Haem iron coordination | Axial iron ligands | Formal iron oxidation/spin states |
|---|---|---|---|
![]() | ![]() |
His;
S |
FeII (S=0);
FeIII (S=1/2) |
Cytochromes b (cyt b) can be defined as electrontransfer proteins having one or two haem b groups, noncovalently bound to the protein. The fifth haem iron ligand is always provided by a histidine residue. Cyt b possess a wide range of properties and function in a large number of different redox processes [1].
A number of cytochromes with very different sequences and haem coordination
centres share a common 3D structure, namely
a four
helix lefttwisted
antiparallel bundle [2]. This group includes
soluble cyt b562, cyt b557
(bacterioferritin), and Class II cyt c.
Although soluble cyt b562 from the periplasm of
Escherichia coli has this characteristic chain fold, its sequence
bears no similarity to the other
four
helix bundle
cytochromes. The protein consists of four nearly parallel
helices; the haem group is
inserted between the helices near one end of the molecule with one heme
face partially exposed to solvent (see Figure 256B).
Histidine and methionine provide the fifth and sixth haem ligands
[3].
| C562_ECOLI | Soluble cytochrome b562 precursor; Escherichia coli |
| Protein Superfamily | Pfam | LPFC 3D alignment |
|---|---|---|
| 00018; cytochrome b562 |
| PDB | scop | BSM | RELI Base | Header |
¹ |
|---|---|---|---|---|---|
| 1apc¶ | 1apc¶ | 1apc¶ | 1apc | Cytochrome b562 (apo form); Escherichia coli | MS5IB4 |
| 256b | 256b | 256b | 256b | Cytochrome b562 (oxidised) (complex with sulphate); Escherichia coli |
¹ Macromolecular Structures abstract.
Full text is available to BioMedNet
Members
References
helical bundle
cytochromes.
Biochim. Biophys. Acta 1058, 38-41.
|
| Bibliography on structural studies of soluble cytochrome b562 |