Hemoglobin and Cyanide

[Bob Hoesch]

In article <4a4le3$d1n at newserv.ksu.ksu.edu> "Dr. Laura A. Andersson" <laraheme at KSUVM.KSU.EDU> writes:
>From: "Dr. Laura A. Andersson" <laraheme at KSUVM.KSU.EDU>
>Subject: Re: Hemoglobin and Cyanide
>Date: 6 Dec 1995 17:55:15 GMT

> the "reduction" is not 
>a redox reaction, but a "decrease" (also a reduction) in amount of metMb. With 
>respect to number of hemoglobin bands, first metHb has bands at 405 (Soret) 500 & 
>629 nm, with millimolar extinction coefficients, respectively, of 179, 10, and 4.4. 
> but for cyanometHb, the bands are at 418 and 541 nm, with millimolar extinction 
>coefficeints of 124 and 12.5 nm.  key point - the "high-spin" marker at 629 is 
>GONE if the cyanide form is complete. [Hb has a high affinity for cyanide - only 
>need ~10 x to be complete.]

This makes sense in terms of a change in the number of spectrophotometric 
absorption peaks, but I still don't think we have a good explanation for the 
reduction in the number of electrophoretic bands.  After all, the protein 
doesn't go away.