Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases

摘要: Dye decolorizing peroxidases (DyPs) are novel haem-containing peroxidases, which structurally unrelated to classical peroxidases. They lack the highly conserved distal histidine that acts as an acid-base catalyst in catalytic reaction of implies distinct mechanistic properties. Despite remarkable properties and recognized potential for biotechnology applications, knowledge DyP's structural features solution, govern reactivity catalysis, is lagging behind. Resonance Raman (RR) spectroscopy can reveal fine details active site structure hemoproteins, reporting on oxidation spin state coordination haem cofactor. We provide overview binding pocket architecture enzymes from A, B C DyP subfamilies, light those established search subfamily specific among DyPs. RR demonstrates multiple populations typically co-exist DyPs, like case The spin/coordination strongly pH dependent correlates well with respective Unlike a surprisingly high abundance catalytically incompetent low population observed several tentatively related alternative physiological function these enzymes. molecular sites elucidated by spectroscopy, furthermore guide approaches biotechnological exploitation promising biocatalysts.