Thermodynamics of hydrogen cyanide and hydrogen fluoride binding to cytochrome c peroxidase and its Asn-82-->Asp mutant.

doi:10.1042/bj3020437

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Article

Thermodynamics of hydrogen cyanide and hydrogen fluoride binding to cytochrome c peroxidase and its Asn-82-->Asp mutant.

The Biochemical journal - 1 Sept 1994

DeLauder S F, Mauro J M, Poulos T L, Williams J C, Schwarz F P

Abstract excerpt

The thermodynamics of binding of fluoride and cyanide to cytochrome c peroxidase (CCP) and its Asn-82-->Asp mutant (D82CCP) in phosphate and acetate buffer at an ionic strength of 0.15 mol.kg-1 from pH 5.0 to 7.1 were investigated by titration calorimetry at 289 and 297 K. The binding reactions a...

Topics

Asparagine
Binding Sites
Buffers
Calorimetry
Cytochrome-c Peroxidase
Hydrofluoric Acid
Hydrogen Cyanide
Mutation
Spectrophotometry, Ultraviolet
Thermodynamics

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