作者: Toru Shimizu , Alzbeta Lengalova , Václav Martínek , Markéta Martínková
DOI: 10.1039/C9CS00268E
关键词: Hemeprotein 、 Signal transduction 、 Heme 、 Cytochrome P450 、 Cytochrome 、 Myoglobin 、 Protein degradation 、 Cofactor 、 Biochemistry 、 Chemistry
摘要: Protoporphyrin IX iron complex (heme) is an important cofactor for oxygen transfer, storage, activation, and electron transfer when bound to the heme proteins hemoglobin, myoglobin, cytochrome P450 c, respectively. In addition these prototypical proteins, there are emergent, critical roles of exchangeable/labile in signal transduction. Specifically, it has been shown that association/dissociation to/from heme-responsive sensors regulates numerous functions, including transcription, DNA binding, microRNA splicing, translation, protein kinase activity, degradation, K+ channel function, two-component transduction, many other functions. this review, we provide a comprehensive overview structure–function relationships describe new, additional as functional inhibitors activators. order complete description various heme-bound also mention novel chemical reaction centre aldoxime dehydratase, cis–trans isomerase, N–N bond formation, hydrazine formation S–S These unprecedented functions should be interest biological chemists. Insight into underlying molecular mechanisms essential understanding new role physiological pathological processes.