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Title: Effect of ligands on cytochrome d from Azotobacter vinelandii

Journal Article · · J. Bioenerg. Biomembr.; (United States)
DOI:https://doi.org/10.1007/BF00744688· OSTI ID:6056636

Spectra of oxidized and reduced cytochrome d in particles of A. vinelandii were studied in the presence of the ligands CO, azide, and NH2OH under oxidizing, reducing, and turnover conditions. Under oxidizing conditions, spectral changes were observed on oxidized cytochrome d in the presence of CO and NH2OH showing a shift of the maximum to shorter wavelengths. Under reducing conditions, spectral changes were observed on reduced cytochrome d in the presence of CO, NO, NO2-, and NH2OH. Under turnover conditions CO, NH2OH, and azide cause a spectral shift of the absorption maximum of cytochrome d. The spectral changes caused by CO and NH2OH were interpreted as a binding of the ligands to cytochrome d changing its conformation from the oxidized state absorbing at 648 nm into a more stable liganded form. Since azide does not affect the spectral bands of oxidized and reduced cytochrome d, the spectral change during turnover in the presence of azide were ascribed to a preferential binding of azide to enzymically active conformation of cytochrome d (cytochrome dx).

Research Organization:
Jansen Inst. Univ. of Amsterdam, Netherlands
OSTI ID:
6056636
Journal Information:
J. Bioenerg. Biomembr.; (United States), Vol. 12:3-4
Country of Publication:
United States
Language:
English