What question did this study set out to answer?

To identify and compare the electronic structures and reaction pathways of reactive oxygen intermediates formed upon the reduction of oxy-heme oxygenase and oxy-myoglobin.

January 10, 2007Journal of the American Chemical Society

Distinct Reaction Pathways Followed upon Reduction of Oxy-Heme Oxygenase and Oxy-Myoglobin as Characterized by Mössbauer Spectroscopy

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Authors

RGRicardo García‐SerresCentre National de la Recherche Scientifique RDRoman DavydovPeter the Great St. Petersburg Polytechnic University TMToshitaka MatsuiTohoku University

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Implication

Biophysical study uncovers divergent oxygen-activation pathways in reduced oxy-heme oxygenase and oxy-myoglobin, demonstrating that protein structure dictates reactive intermediate formation.

Key Points

To identify and compare the electronic structures and reaction pathways of reactive oxygen intermediates formed upon the reduction of oxy-heme oxygenase and oxy-myoglobin.
Generated reactive oxygen intermediates via 77 K radiolytic cryoreduction of oxy-heme oxygenase and oxy-myoglobin followed by progressive thermal annealing.
Characterized electronic states, intermediate configurations, and reaction products using Mössbauer and electron paramagnetic resonance spectroscopies.
One-electron reduction of oxy-heme oxygenase accompanied by protonation produced a low-spin ferric-hydroperoxo intermediate that self-hydroxylated directly to alpha-meso-hydroxyhemin without forming a ferryl species.
One-electron reduction of oxy-myoglobin produced an unprotonated peroxo species that, upon protonation, yielded a ferric-hydroperoxo intermediate and subsequently decayed into a ferryl complex possessing compound II-like magnetic properties.
The spectroscopic evidence directly identifies ferric-hydroperoxo hemes as the precursors of reactive ferryl species in oxygen activation, highlighting that protein architecture governs pathway divergence.

Cite This Study

García‐Serres et al. (2007) studied this question.

synapsesocial.com/papers/6a83882cbffc6f8cb851941b https://doi.org/10.1021/ja067209i

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Implication

Biophysical study uncovers divergent oxygen-activation pathways in reduced oxy-heme oxygenase and oxy-myoglobin, demonstrating that protein structure dictates reactive intermediate formation.

Distinct Reaction Pathways Followed upon Reduction of Oxy-Heme Oxygenase and Oxy-Myoglobin as Characterized by Mössbauer Spectroscopy

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Implication

Key Points

Cite This Study

Distinct Reaction Pathways Followed upon Reduction of Oxy-Heme Oxygenase and Oxy-Myoglobin as Characterized by Mössbauer Spectroscopy

Discussion

Member takes

Implication

Key Points

Cite This Study

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