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- W2003266182 abstract "Resonance Raman and infrared spectroscopy have been used to characterize the vibrational modes of CO-bound horseradish peroxidase (HRP) and cytochrome c peroxidase (CCP). At low pH both proteins show two forms attributed to linear non-H-bonded CO (form I) and tilted CO which is H-bonded with a distal residue (form II). The frequencies differ between the two proteins and indicate that H bonding is weaker for CCP. The equilibrium between the two forms depends on the CO pressure. This suggests a secondary binding to CO that perturbs the distal residue. At high pH only one form is observed. Whereas HRPCO shows form I, a new conformer, form II′, is observed for CCP. A tilted non-H-bonded CO is suggested." @default.
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- W2003266182 date "1986-03-01" @default.
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- W2003266182 title "Two CO binding modes for HRPCO and CCPCO: Raman evidence of CO pressure and pH dependence" @default.
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- W2003266182 doi "https://doi.org/10.1016/0022-2860(86)80358-1" @default.
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