
thumbnail|right|The structure of cytochrome b5 reductase, the enzyme that converts methemoglobin to hemoglobin.
thumbnail|right|The structure of cytochrome b5 reductase, the enzyme that converts methemoglobin to hemoglobin.
Methemoglobin (British: methaemoglobin, shortened MetHb) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe3+ (ferric) state, not the Fe2+ (ferrous) of normal hemoglobin. Sometimes, it is also referred to as ferrihemoglobin. Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues. It is bluish chocolate-brown in color. In human blood a trace amount of methemoglobin is normally produced spontaneously, but when present in excess the blood becomes abnormally dark bluish brown. The NADH-dependent enzyme methemoglobin reductase (a type of diaphorase) is responsible for converting methemoglobin back to hemoglobin.
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).