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	XFEL crystal structures of peroxidase compound II Hanna Kwon , Jaswir Basran , Chinar Pathak , Mahdi Hussain , Samuel L. Freeman , Alistair J. Fielding , Anna J. Bailey , Natalia Stefanou , Hazel A. Sparkes , Takehiko Tosha , Keitaro Yamashita , Kunio Hirata , Hironori Murakami , Go Ueno , Hideo Ago , Kensuke Tono , Masaki Yamamoto , Hitomi Sawai , Yoshitsugu Shiro , Hiroshi Sugimoto , Emma Raven , Peter C. E. Moody Angewandte Chemie International Edition DOI: 10.1002/anie.202103010 Open Access Show Abstract ▼ Abstract: 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 IV =O or Fe IV ‐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 IV =O species. For Compound II, the nature of the ferryl heme is not unambiguously established. Here, we report 1.06 Å and 1.50 Å crystal structures for Compound II intermediates in cytochrome c peroxidase (C c P) and ascorbate peroxidase (APX), collected using the X‐ray free electron laser at SACLA. The structures reveal differences between the two peroxidases. The iron‐oxygen bond length in C c P (1.76 Å) is notably shorter than in APX (1.87 Å). The results indicate that the ferryl species is finely tuned across Compound I and Compound II species in closely related peroxidase enzymes. We propose that this fine‐tuning is linked to the functional need for proton delivery to the heme.	Apr 2021

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XFEL crystal structures of peroxidase compound II