Oxygen binding to hemocyanin: a resonance Raman spectroscopic study |
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Authors: | J S Loehr T B Freedman T M Loehr |
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Institution: | Department of Chemistry, Portland State University, Portland, OR 97207 USA;Department of Chemistry, Oregon Graduate Center, Beaverton, OR 97005 USA |
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Abstract: | Oxygenation of hemocyanin gives rise to resonance Raman peaks at 742 and 282 cm?1. The 742 cm?1 peak which is in resonance with the 575 nm charge transfer band shifts to 704 cm?1 when 18O2 is substituted for 16O2. Our results establish that the bound oxygen is in the form of peroxide (O22?). The 282 cm?1 peak which is in resonance with the 340 nm optical transition is insensitive to isotopic substitution, suggesting that the 282 cm?1 peak corresponds to a vibration involving the magnetically-coupled Cu(II)··Cu(II) centers. |
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