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<p>The use of X-ray structures to determine and interpret the ferryl iron-oxygen bond order in molecular oxygen-activating heme enzymes has, in the past, been controversial. This has mainly stemmed from the susceptibility of ferryl species to X-ray-induced electronic state changes. In this work we establishe using time-resolved serial femtosecond X-ray crystallography (tr-SFX) on a dye-decolourising peroxidase that the ferryl intermediate species (Compounds I and II) captured following in situ mixing of microcrystals with H<sub>2</sub>O<sub>2</sub> have single, rather than the double bond character expected. X-ray emission validated tr-SFX data with quantum refinement, time-dependent-DFT calculations and QM/MM geometry optimizations together support the concept that the single iron-oxygen bond character is not an indication of ferryl reduction or a protonated form (Fe<sup>IV</sup>-OH) but is instead attributed to the existence of accessible excited states possessing ferric-oxyl (Fe<sup>III</sup>–O<sup>•–</sup>) character. Such states offer insight into the nature of ferryl heme.</p>

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Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月3日

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  • Lewis J. Williams,
  • Jos J.A.G. Kamps,
  • Adrian M. V. Brânzanic,
  • Maria Lehene,
  • Kristoffer J. M. Lundgren,
  • Ulf Ryde,
  • Kuntal Chatterjee,
  • Margaret D. Doyle,
  • Philipp S. Simon,
  • Hiroki Makita,
  • Amy J. Thompson,
  • Aaron S. Brewster,
  • Tiankun Zhou,
  • Marina Lučić,
  • Michael T. Wilson,
  • Pierre Aller,
  • Juan Sanchez-Weatherby,
  • Leland Gee,
  • Sebastian Dehe,
  • Sandra Mous,
  • Junko Yano,
  • Vittal K. Yachandra,
  • Michael A. Hough,
  • Allen M. Orville,
  • Jan F. Kern,
  • Radu L. Silaghi-Dumitrescu,
  • Jonathan A. R. Worrall

摘要

The use of X-ray structures to determine and interpret the ferryl iron-oxygen bond order in molecular oxygen-activating heme enzymes has, in the past, been controversial. This has mainly stemmed from the susceptibility of ferryl species to X-ray-induced electronic state changes. In this work we establishe using time-resolved serial femtosecond X-ray crystallography (tr-SFX) on a dye-decolourising peroxidase that the ferryl intermediate species (Compounds I and II) captured following in situ mixing of microcrystals with H2O2 have single, rather than the double bond character expected. X-ray emission validated tr-SFX data with quantum refinement, time-dependent-DFT calculations and QM/MM geometry optimizations together support the concept that the single iron-oxygen bond character is not an indication of ferryl reduction or a protonated form (FeIV-OH) but is instead attributed to the existence of accessible excited states possessing ferric-oxyl (FeIII–O•–) character. Such states offer insight into the nature of ferryl heme.