NDLI: Peculiarities of cyanide binding to the ba 3-type cytochrome oxidase from the thermophilic bacterium Thermus thermophilus

Content Provider	Springer Nature Link
Author	Kalivich, A. V. Azarkina, N. V. Vygodina, T. V. Soulimane, T. Konstantiv, A. A.
Copyright Year	2010
Abstract	Cytochrome c oxidase of the ba 3-type from Thermus thermophilus does not interact with cyanide in the oxidized state and acquires the ability to bind heme iron ligands only upon reduction. Cyanide complexes of the reduced heme a 3 in cytochrome ba 3 and in mitochondrial aa 3-type cytochrome oxidase are similar spectroscopically, but the a 32+-CN complex of cytochrome ba 3 is strikingly tight. Experiments have shown that the K d value of the cytochrome ba 3 complex with cyanide in the presence of reductants of the enzyme binuclear center does not exceed 10−8 M, which is four to five orders of magnitude less than the K d of the cyanide complex of the reduced heme a 3 of mitochondrial cytochrome oxidase. The tightness of the cytochrome ba 3 complex with cyanide is mainly associated with an extremely slow rate of the ligand dissociation (k off ≤ 10−7 sec−1), while the rate of binding (k on ∼ 102 M−1·sec−1) is similar to the rate observed for the mitochondrial cytochrome oxidase. It is proposed that cyanide dissociation from the cytochrome ba 3 binuclear center might be hindered sterically by the presence of the second ligand molecule in the coordination sphere of CuB2+. The rate of cyanide binding with the reduced heme a 3 does not depend on pH in the neutral area, but it approaches linear dependence on H+ activity in the alkaline region. Cyanide binding appears to be controlled by protonation of an enzyme group with pK a = 8.75.
Starting Page	342
Ending Page	352
Page Count	11
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	75
Issue Number	3
e-ISSN	16083040
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2010-03-24
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	cytochrome oxidase ba 3 cyanide hemoproteins oxygen reducing center Thermus thermophilus Biomedicine general Microbiology Bioorganic Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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