| Description | In Gram-negative bacteria, growth on methanol is dependent on the soluble, periplasmic quinoprotein methanol dehydrogenase, which oxidises methanol to formaldehyde. The electrons generated by this reaction are transferred from the reduced enzyme to the unusual cytochrome cL, which is subsequently oxidised itself by cytochrome c2 (also known as cytochrome cH), which then transfers the electrons to a membrane-bound cytochrome oxidase [ ].This entry represents cytochrome cL (also known as cytochrome C551i in some species), whose amino acid sequence is distinct from that of other c-type cytochromes and does not fit into any established amino acid sequence class. Despite its lack of homology to other proteins, many of its properties, eg the low-spin haem prosthetic group, are similar to those of class 1 cytochrome c proteins. Other properties, such as its large size and acidic nature are distinct to cytochrome cL. The core of this protein has a structure typical of class I cytochrome c proteins, consisting of compact α helices enclosing the haem c prosthetic group with one edge of the haem exposed [ ]. Unusually, there is a tightly bound calcium close to the haem group which is thought to help stabilise redox potential and may be involved in the transfer of electrons from methanol dehydrogenase to the haem group. | Name | Cytochrome cL |
| Short Name | Cyt_cL | Type | Family |
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