Biochemical analysis demonstrates how active-site hydrogen bonding modulates ferryl reactivity in heme peroxidase, indicating key structural controls on metal-oxo catalysis.
. Our data highlight how Trp51 tunes the lifetimes of key ferryl intermediates and works in synergy with the redox active Trp191 and a well-defined substrate binding site to regulate catalytic function. More broadly, this work shows how noncanonical substitutions can advance our understanding of active site features governing metal-oxo structure and reactivity.
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Ortmayer et al. (2021) studied this question.
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