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XFEL crystal structures of peroxidase compound II

DOI: 10.1002/anie.202103010 DOI Help

Authors: Hanna Kwon (University of Bristol) , Jaswir Basran (University of Leicester) , Chinar Pathak (University of Leicester) , Mahdi Hussain (University of Leicester) , Samuel L. Freeman (University of Bristol) , Alistair J. Fielding (Liverpool John Moores University) , Anna J. Bailey (University of Bristol) , Natalia Stefanou (University of Bristol) , Hazel A. Sparkes (University of Bristol) , Takehiko Tosha (RIKEN SPring-8 Center) , Keitaro Yamashita (MRC Laboratory of Molecular Biology) , Kunio Hirata (RIKEN SPring-8 Center) , Hironori Murakami (Japan Synchrotron Radiation Research Institute) , Go Ueno (RIKEN SPring-8 Center) , Hideo Ago (RIKEN SPring-8 Center) , Kensuke Tono (Japan Synchrotron Radiation Research Institute) , Masaki Yamamoto (RIKEN SPring-8 Center) , Hitomi Sawai (University of Hyogo) , Yoshitsugu Shiro (University of Hyogo) , Hiroshi Sugimoto (RIKEN SPring-8 Center) , Emma Raven (University of Bristol) , Peter C. E. Moody (University of Leicester)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition

State: Published (Approved)
Published: April 2021

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.

Journal Keywords: Heme proteins; heme; peroxidase

Subject Areas: Chemistry, Biology and Bio-materials

Facility: XFEL at SACLA

Added On: 13/04/2021 10:32

Discipline Tags:

Organic Chemistry Life Sciences & Biotech Chemistry Biochemistry

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