Nature communications · 2026
Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?
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Williams Lewis J, Kamps Jos J A G, Brânzanic Adrian M V, Lehene Maria, Lundgren Kristoffer J M, Ryde Ulf, Chatterjee Kuntal, Doyle Margaret D, Simon Philipp S, Makita Hiroki, Thompson Amy J, Brewster Aaron S, Zhou Tiankun, Lučić Marina, Wilson Michael T, Aller Pierre, Sanchez-Weatherby Juan, Gee Leland, Dehe Sebastian, Mous Sandra, Yano Junko, Yachandra Vittal K, Hough Michael A, Orville Allen M, Kern Jan F, Silaghi-Dumitrescu Radu L, Worrall Jonathan A R
Аннотация
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.