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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 30, Number 4
BKCSDE 30(4)
April 20, 2009

Title	Rebinding Dynamics of CO Following Photodissociation of 4.0 M Guanidine HCl-Denatured Carbonmonoxyhemoglobin
Author	Jaeheung Park, Taegon Lee, Jooyoung Kim, Salina A Chowdhurry, Manho Lim*
Keywords	CO rebinding, Hemoglobin, Guanidine HCl, Femtosecond vibrational spectroscopy, Denaturation
Abstract	Femtosecond vibrational spectroscopy was used to probe the dynamics of CO rebinding to hemoglobin (Hb), denatured by 4.0 M GdnHCl in D₂O at 283 K, after photolysis of HbCO. The stretching mode of ¹³CO bound to the denatured Hb¹³CO showed a single band centered at 1922 cm^-1, indistinguishable from that of denatured Mb¹³CO. 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.
Page	913 - 916
Full Text	PDF

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