Ontology highlight
ABSTRACT:
SUBMITTER: Kwon H
PROVIDER: S-EPMC8251747 | biostudies-literature | 2021 Jun
REPOSITORIES: biostudies-literature
Kwon Hanna H Basran Jaswir J Pathak Chinar C Hussain Mahdi M Freeman Samuel L SL Fielding Alistair J AJ Bailey Anna J AJ Stefanou Natalia N Sparkes Hazel A HA Tosha Takehiko T Yamashita Keitaro K Hirata Kunio K Murakami Hironori H Ueno Go G Ago Hideo H Tono Kensuke K Yamamoto Masaki M Sawai Hitomi H Shiro Yoshitsugu Y Sugimoto Hiroshi H Raven Emma L EL Moody Peter C E PCE
Angewandte Chemie (International ed. in English) 20210519 26
Oxygen activation in all heme enzymes requires the formation of high oxidation states of iron, usually referred to as ferryl heme. There are two known intermediates: Compound I and Compound II. The nature of the ferryl heme-and whether it is an Fe<sup>IV</sup> =O or Fe<sup>IV</sup> -OH species-is important for controlling reactivity across groups of heme enzymes. The most recent evidence for Compound I indicates that the ferryl heme is an unprotonated Fe<sup>IV</sup> =O species. For Compound II, ...[more]