Kwon, H, Basran, J, Pathak, C, Hussain, M, Freeman, SL, Fielding, AJ, Bailey, AJ, Stefanou, N, Sparkes, HA, Tosha, T, Yamashita, K, Hirata, K, Murakami, H, Ueno, G, Ago, H, Tono, K, Yamamoto, M, Sawai, H, Shiro, Y, Sugimoto, H et al, Raven, E and Moody, PCE (2021) XFEL Crystal Structures of Peroxidase Compound II. Angewandte Chemie International Edition. ISSN 1521-3773

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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.

Item Type:	Article
Uncontrolled Keywords:	03 Chemical Sciences
Subjects:	R Medicine > RS Pharmacy and materia medica
Divisions:	Pharmacy & Biomolecular Sciences
Publisher:	Wiley
Related URLs:	Author
Date Deposited:	02 Jun 2021 15:44
Last Modified:	04 Sep 2021 05:35
DOI or ID number:	10.1002/anie.202103010
URI:	https://researchonline.ljmu.ac.uk/id/eprint/14823

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