Cytochrome f: Difference between revisions

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<StructureSection load='1ctm' size='350' side='right' caption='Turnip heme-containing cytochrome f (PDB entry [[1ctm]])' scene='48/484838/Cv/8'>
<StructureSection load='' size='350' side='right' caption='Turnip heme-containing cytochrome f (PDB entry [[1ctm]])' scene='48/484838/Cv/8'>


'''Cytochrome f''' (Cytf) is the largest subunit of the cytochrome b6f complex.  This complex transfers electrons from plastocyanin to the two reaction center complexes of oxygenic photosynthetic membranes.<ref>PMID:7631417</ref>
'''Cytochrome f''' (Cytf) is the largest subunit of the cytochrome b6f complex.  This complex transfers electrons from plastocyanin to the two reaction center complexes of oxygenic photosynthetic membranes.<ref>PMID:7631417</ref>


 
See also [[Hemeproteins]].


== Structural highlights ==
== Structural highlights ==
Line 9: Line 9:
The cytochrome b6f complex contains 4 subunits: Cytf, Cytb6, Rieske iron-sulfur protein and subunit IV.  Cytf has an internal chain of water molecules conserved in all its 3D structures.  The water chain is assumed to be a proton wire.
The cytochrome b6f complex contains 4 subunits: Cytf, Cytb6, Rieske iron-sulfur protein and subunit IV.  Cytf has an internal chain of water molecules conserved in all its 3D structures.  The water chain is assumed to be a proton wire.


<scene name='48/484838/Cv/9'>Heme binding site</scene> in Turnip cytochrome f
<scene name='48/484838/Cv/12'>Heme binding site</scene> in Turnip cytochrome f


<scene name='48/484838/Cv/10'>Covalent binding of heme to 2 Cys residues</scene>
<scene name='48/484838/Cv/13'>Covalent binding of heme to 2 Cys residues</scene>


<scene name='48/484838/Cv/11'>Fe coordination site</scene> (PDB entry [[1ctm]]).
<scene name='48/484838/Cv/14'>Fe coordination site</scene> (PDB entry [[1ctm]]).
</StructureSection>
==3D structures of cytochrome f==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==3D structures of cytochrome f==
{{#tree:id=OrganizedByTopic|openlevels=0|
[[Cytochrome f 3D structures]]


*Cytf
</StructureSection>
 
**[[1ctm]], [[1hcz]] – tCytf – turnip<br />
**[[1cfm]] – CrCytf – ''Chlamydomonas reinhardtii''<br />
**[[1e2v]], [[1e2w]], [[1e2z]] – CrCytf (mutant)<br />
**[[1ewh]] - CrCytf soluble domain<br />
**[[1ci3]] - Cytf soluble domain – ''Phormidium laminosum''
 
*Cytf complex with plastocyanin
 
**[[2pcf]] – Cytf soluble domain + plastocyanin – spinach – NMR<br />
**[[1tu2]] - Cytf soluble domain + plastocyanin – Nostoc – NMR<br />
**[[1tkw]] - tCytf soluble domain + plastocyanin – NMR<br />
**[[2jxm]] - Cytf soluble domain + plastocyanin – ''Prochlorothrix hollandica'' – NMR
 
*Full cytochrome b6f containing Cytf


**[[1q90]] – CrCytf <br />
**[[1vf5]], [[2e74]], [[4i7z]] - MlCytf – ''Mastigocladus laminosus''<br />
**[[2d2c]] - MlCytf + dibromo-methyl-isopropylbenzoquinone<br />
**[[2e75]], [[4hoi]] - MlCytf + nonyl-hydroxyquinoline oxide<br />
**[[2e76]], [[4pv1]], [[4h13]] - MlCytf + stigmatellin derivative<br />
**[[2zt9]], [[4ogq]], [[4h44]] - Cytf - Nostoc<br />
**[[5cxm]] – Cytf – ''Synechocystis''<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Latest revision as of 14:24, 9 January 2020


Cytochrome f (Cytf) is the largest subunit of the cytochrome b6f complex. This complex transfers electrons from plastocyanin to the two reaction center complexes of oxygenic photosynthetic membranes.[1]

See also Hemeproteins.

Structural highlights

The cytochrome b6f complex contains 4 subunits: Cytf, Cytb6, Rieske iron-sulfur protein and subunit IV. Cytf has an internal chain of water molecules conserved in all its 3D structures. The water chain is assumed to be a proton wire.

in Turnip cytochrome f

(PDB entry 1ctm).

3D structures of cytochrome f

Cytochrome f 3D structures


Turnip heme-containing cytochrome f (PDB entry 1ctm)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Prince RC, George GN. Cytochrome f revealed. Trends Biochem Sci. 1995 Jun;20(6):217-8. PMID:7631417

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Michal Harel, Alexander Berchansky, Joel L. Sussman