NDLI: Binding of Imidazole to the Heme of Cytochrome c 1 and Inhibition of the bc 1 Complex from Rhodobacter sphaeroides

Content Provider	PubMed Central
Author	Oleksandr, Kokhan Shinkarev, Vladimir P. Wraight, Colin A.
Abstract	We have used imidazole (Im) and N-methylimidazole (MeIm) as probes of the heme-binding cavity of membrane-bound cytochrome (cyt) c 1 in detergent-solubilized bc 1 complex from Rhodobacter sphaeroides. Imidazole binding to cyt c 1 substantially lowers the midpoint potential of the heme and fully inhibits bc 1 complex activity. Temperature dependences showed that binding of Im (Kd ≈ 330 μm, 25 °C, pH 8) is enthalpically driven (ΔH 0 = −56 kJ/mol, ΔS 0 = −121 J/mol/K), whereas binding of MeIm is 30 times weaker (Kd ≈ 9.3 mm) and is entropically driven (ΔH 0 = 47 kJ/mol, ΔS 0° = 197 J/mol/K). The large enthalpic and entropic contributions suggest significant structural and solvation changes in cyt c 1 triggered by ligand binding. Comparison of these results with those obtained previously for soluble cyts c and c 2 suggested that Im binding to cyt c 1 is assisted by formation of hydrogen bonds within the heme cleft. This was strongly supported by molecular dynamics simulations of Im adducts of cyts c, c 2, and c 1, which showed hydrogen bonds formed between the NδH of Im and the cyt c 1 protein, or with a water molecule sequestered with the ligand in the heme cleft.
Related Links	http://dx.doi.org/10.1074/jbc.m110.128058
Ending Page	22521
Page Count	9
Starting Page	22513
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	29
Volume Number	285
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2010-07-16
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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