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Title: Anomalously slow cyanide binding to Glycera dibranchiata monomer methemoglobin component II: Implication for the equilibrium constant

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00421a011· OSTI ID:7189724
;  [1]
  1. Univ. of New Mexico, Albuquerque (USA)

In comparison to sperm whale metmyoglobin, metleghemoglobin {alpha}, methemoglobins, and heme peroxidases, the purified Glycera dibranchiata monomer methemoglobin component II exhibits anomalously slow cyanide ligation kinetics. For the component II monomer methemoglobin this reaction has been studied under pseudo-first-order conditions at pH 6.0, 7.0, 8.0, and 9.0, employing 100-250-fold mole excesses of potassium cyanide at each pH. The analysis shows that the concentration-independent bimolecular rate constant is small in comparison to those of the other heme proteins. Furthermore, the results show that the dissociation rate is extremely slow. Separation of the bimolecular rate constant into contributions from k{sub CN{sup {minus}}} (the rate constant for CN{sup {minus}} binding) and from k{sub HCN} (the rate constant for HCN binding) shows that the former is approximately 90 times greater. These results indicate that cyanide ligation reactions are not instantaneous for this protein, which is important for those attempting to study the ligand-binding equilibria. From the results presented here the authors estimate that the actual equilibrium dissociation constant (K{sub D}) for cyanide binding to this G. dibranchiata monomer methemoglobin has a numerical upper limit that is at least 2 orders of magnitude smaller than the value reported before the kinetic results were known.

OSTI ID:
7189724
Journal Information:
Biochemistry; (USA), Vol. 27:21; ISSN 0006-2960
Country of Publication:
United States
Language:
English