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XFEL Crystal Structures of Peroxidase Compound II.

Hanna Kwon1, Jaswir Basran2, Chinar Pathak2

  • 1School of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.

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|March 20, 2024
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Summary
This summary is machine-generated.

High-resolution crystal structures reveal distinct Compound II ferryl heme intermediates in cytochrome c peroxidase and ascorbate peroxidase. This fine-tuning is crucial for enzyme function and proton delivery.

Keywords:
hemeheme proteinsperoxidase

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Heme enzymes activate oxygen via high-valent iron species, known as ferryl heme intermediates.
  • Compound I and Compound II are key intermediates, with their precise nature influencing enzyme reactivity.
  • The exact structure of Compound II ferryl heme remains incompletely understood.

Purpose of the Study:

  • To elucidate the structural characteristics of Compound II ferryl heme intermediates in cytochrome c peroxidase (CcP) and ascorbate peroxidase (APX).
  • To investigate the differences in ferryl heme structure between these two closely related peroxidase enzymes.
  • To explore the functional implications of structural variations in ferryl heme species.

Main Methods:

  • High-resolution (1.06 Å and 1.50 Å) crystal structure determination of Compound II intermediates.
  • Utilizing the X-ray free electron laser (XFEL) at SACLA for data collection.
  • Comparative structural analysis of CcP and APX Compound II intermediates.

Main Results:

  • Distinct crystal structures were obtained for Compound II intermediates in CcP and APX.
  • A significant difference in iron-oxygen bond length was observed: 1.76 Å in CcP versus 1.87 Å in APX.
  • These findings highlight structural heterogeneity in ferryl heme species even within related peroxidases.

Conclusions:

  • The ferryl heme species in Compound II are structurally distinct between CcP and APX.
  • This structural fine-tuning of ferryl heme is likely linked to the specific proton delivery requirements of each enzyme.
  • Understanding these variations provides insight into the catalytic mechanisms of heme enzymes.