Cytochrome b562 is a small, soluble, four-helix-bundle protein with a single b-type heme cofactor originally described by Itagaki and Hagar. The protein has been well characterized both structurally and biophysically. In b-type cytochromes, the heme is not covalently attached to the protein, which is the case in the c-type cytochromes. This noncovalent attachment means that the heme is easily removed and apocytochrome b562 can be reconstituted with a range of nonheme porphyrins. Here you can see a recent crystal structure of the Escherichia coli cytochrome b562 (PDB code: 8DRJ)
#molecularart ... #immolecular ... #cytochrome ... #b562 ... #heme ... #crystal ... #redox
Structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #cytochrome ... #b562 ... #heme ... #crystal ... #redox
Structure rendered with @proteinimaging and depicted with @corelphotopaint
