Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Rebinding Dynamics of CO Following Photodissociation of 4.0 M Guanidine HCl-Denatured Carbonmonoxyhemoglobin

  • Park, Jae-Heung (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University) ;
  • Lee, Tae-Gon (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University) ;
  • Kim, Joo-Young (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University) ;
  • Chowdhurry, Salina A. (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University) ;
  • Lim, Man-Ho (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University)
  • Published : 2009.04.20
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Abstract

Femtosecond vibrational spectroscopy was used to probe the dynamics of CO rebinding to hemoglobin (Hb), denatured by 4.0 M GdnHCl in $D_2O# at 283 K, after photolysis of HbCO. The stretching mode of $^{13}CO$ bound to the denatured $Hb^{13}CO$ showed a single band centered at 1922 $cm^{-1}$, indistinguishable from that of denatured $Mb^{13}CO$. Geminate rebinding of CO to the denatured Hb was accelerated more than 1000 times, suggesting that the native structure of the Hb is required to suppress efficient geminate rebinding of CO, as is the case in Mb. The geminate yield and rate for CO rebinding are almost the same in both the denatured Hb and Mb. Similarity in the equilibrium spectrum and rebinding dynamics of CO indicates that the state of the denatured Hb is very similar to that of the denatured Mb. In the denatured Hb, quaternary contact of the protein is likely severed, with the denatured protein existing as an independent subunit much like Mb.

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