Cytochrome b

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Cytochrome b, N-terminal transmembrane domain
TCDB
3.D.3
OPM superfamily3
OPM protein3h1j
CDDcd00284
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cytochrome b, C-terminal domain
cytochrome bc1 complex
Identifiers
SymbolCytochrom_B_C
PfamPF00032
InterProIPR005798
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cytochrome b within both

proton gradient is used for the generation of ATP. These complexes play a vital role in cells.[1][2][3]

Structure and function

b/b6 is an integral

ligands of the iron atoms of these two heme groups.[2][3]

The heme groups are key parts of the internal electron transfer pathway and indespensible to the functioning of the two quinol oxidizing complexes. Two units of b/b6 also form a quinol entry pathway.[4]

Use in phylogenetics

Cytochrome b is commonly used as a region of

phylogenetic relationships between organisms, due to its sequence variability. It is considered to be most useful in determining relationships within families and genera. Comparative studies involving cytochrome b have resulted in new classification schemes and have been used to assign newly described species to a genus as well as to deepen the understanding of evolutionary relationships.[5]

Clinical significance

Mutations in cytochrome b primarily result in exercise intolerance in human patients; though more rare, severe multi-system pathologies have also been reported.[6]

Single-point mutations in cytochrome b of Plasmodium falciparum and P. berghei are associated with resistance to the anti-malarial drug atovaquone.[7]

Human genes

Human genes encoding cytochrome b proteins include:

  • CYB5A
    – cytochrome b5 type A (microsomal)
  • CYB5B
    – cytochrome b5 type B (outer mitochondrial membrane)
  • CYBASC3 – cytochrome b, ascorbate dependent 3
  • MT-CYB – mitochondrially encoded cytochrome b

Fungicide target

Cyt b is targeted by the

Fungicide Resistance Action Committee group 11. The cyt b mutations G143A and F129L provide resistance against the main body of group 11, although G143A does not work against metyltetraprole (11A).[8] G143A is significant in Botrytis cinerea in California strawberry production.[9]

References

  1. ^ Blankenship, Robert (2009). Molecular Mechanisms of Photosynthesis. Blackwell Publishing. pp. 124–132.
  2. ^
    S2CID 7298013
    .
  3. ^ .
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  8. (PDF) on 2021-11-05. Retrieved 2021-06-16.
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External links