Cytochrome f
Encyclopedia
Cytochrome f is the largest subunit of cytochrome b6f complex
Cytochrome b6f complex
The cytochrome b6f complex is an enzyme found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae, catalyzing the transfer of electrons from plastoquinol to plastocyanin...

 (plastoquinol—plastocyanin reductase; ). In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria. Cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structure
Secondary structure
In biochemistry and structural biology, secondary structure is the general three-dimensional form of local segments of biopolymers such as proteins and nucleic acids...

s.

The 3D structure of Brassica rapa (Turnip) cyt f has been determined. The lumen-side segment of cyt f includes two structural
Secondary structure
In biochemistry and structural biology, secondary structure is the general three-dimensional form of local segments of biopolymers such as proteins and nucleic acids...

 domains: a small one above a larger one that, in turn, is on top of the attachment to the membrane domain. The large domain consists of an anti-parallel beta-sandwich and a short haem-binding peptide, which form a three-layer structure
Protein structure
Proteins are an important class of biological macromolecules present in all organisms. Proteins are polymers of amino acids. Classified by their physical size, proteins are nanoparticles . Each protein polymer – also known as a polypeptide – consists of a sequence formed from 20 possible L-α-amino...

. The small domain is inserted between beta-strands F and G of the large domain and is an all-beta domain. The haem nestles between two short helices
Alpha helix
A common motif in the secondary structure of proteins, the alpha helix is a right-handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier...

 at the N terminus of cyt f. Within the second helix
Helix
A helix is a type of smooth space curve, i.e. a curve in three-dimensional space. It has the property that the tangent line at any point makes a constant angle with a fixed line called the axis. Examples of helixes are coil springs and the handrails of spiral staircases. A "filled-in" helix – for...

 is the sequence motif
Sequence motif
In genetics, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and has, or is conjectured to have, a biological significance...

 for the c-type cytochromes, CxxCH (residues 21-25), which is covalently attached to the haem through thioether bond
Chemical bond
A chemical bond is an attraction between atoms that allows the formation of chemical substances that contain two or more atoms. The bond is caused by the electromagnetic force attraction between opposite charges, either between electrons and nuclei, or as the result of a dipole attraction...

s to Cys-21 and Cys-24. His-25 is the fifth haem iron
Iron
Iron is a chemical element with the symbol Fe and atomic number 26. It is a metal in the first transition series. It is the most common element forming the planet Earth as a whole, forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust...

 ligand
Ligand (biochemistry)
In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. In a narrower sense, it is a signal triggering molecule, binding to a site on a target protein.The binding occurs by intermolecular forces, such as ionic bonds, hydrogen...

. The sixth haem iron ligand
Ligand (biochemistry)
In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. In a narrower sense, it is a signal triggering molecule, binding to a site on a target protein.The binding occurs by intermolecular forces, such as ionic bonds, hydrogen...

 is the alpha-amino group of Tyr-1 in the first helix. Cyt f has an internal network of water
Water
Water is a chemical substance with the chemical formula H2O. A water molecule contains one oxygen and two hydrogen atoms connected by covalent bonds. Water is a liquid at ambient conditions, but it often co-exists on Earth with its solid state, ice, and gaseous state . Water also exists in a...

 molecules that may function as a proton wire. The water chain
Polymer
A polymer is a large molecule composed of repeating structural units. These subunits are typically connected by covalent chemical bonds...

 appears to be a conserved
Conserved sequence
In biology, conserved sequences are similar or identical sequences that occur within nucleic acid sequences , protein sequences, protein structures or polymeric carbohydrates across species or within different molecules produced by the same organism...

feature of cyt f.

External links

- X-ray structure of lumen-side domain of cytochrome f from turnip (Brassica rapa) - X-ray structure of lumen-side domain of cytochrome f from Chlamydomonas reinhardtii - X-ray tructure of soluble domain of cytochrome f from cyanobacterium Phormidium laminosum - InterPro entry for cytochrome f
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