¹⁹F NMR Study of b-Type Haemoproteins

Because of their ubiquitousness and abundance as well as their many unique physicochemical properties arising primarily from the presence of a haem group, usually an iron-protoporphyrin IX complex (protohaem; structure shown in Fig. 1A), haemoproteins are the most studied group of proteins. Haem is the prosthetic group of a number of proteins possessing remarkably different functions, i.e. oxygen storage or transport proteins (myoglobin (Mb) or haemoglobin), electron transfer proteins (cytochromes, etc.), oxidase enzymes (peroxidase, catalase, etc.), and gas sensor proteins (Fix L [1], Haem AT [2], etc.). Since these proteins contain the same prosthetic group at their active sites, their functional differences are thought to arise from differences in the way that they interact with the haem.