期刊
JOURNAL OF PORPHYRINS AND PHTHALOCYANINES
卷 20, 期 1-4, 页码 134-149出版社
WORLD SCIENTIFIC PUBL CO PTE LTD
DOI: 10.1142/S1088424616300081
关键词
protoheme; globin; fold; myoglobin; hemoglobin; evolution
If life without heme-Fe were at all possible, it would definitely be different. Indeed this complex and versatile iron-porphyrin macrocycle upon binding to different globins yields hemeproteins crucial to sustain a variety of vital functions, generally classified, for convenience, in a limited number of functional families. Over-and-above the array of functions briefly outlined below, the spectacular progress in molecular genetics seen over the last 30 years led to the discovery of many hitherto unknown novel hemeproteins in prokaryotes and eukaryotes. Here, we highlight a few basic aspects of the chemistry of the hemeprotein universe, in particular those that are relevant to the control of heme-Fe reactivity and specialization, as sculpted by a variety of interactions with the protein moiety.
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