Effect of ligands on cytochrome d from Azotobacter vinelandii
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
Similar Records
Comparative carbon-13, nitrogen-15, and phosphorus-31 nuclear magnetic resonance study on the flavodoxins from Clostridium MP, Megasphaera elsdenii, and Azotobacter vinelandii
Effects of the Tyr-67 acetylation on the heme crevice structure of horse heart cytochrome c derivatives
Related Subjects
AZIDES
PHARMACOLOGY
CARBON MONOXIDE
CYTOCHROMES
ABSORPTION SPECTRA
HYDROXYLAMINE
AZOTOBACTER
LIGANDS
NITROGEN OXIDES
AMINES
BACTERIA
CARBON COMPOUNDS
CARBON OXIDES
CHALCOGENIDES
MICROORGANISMS
NITROGEN COMPOUNDS
ORGANIC COMPOUNDS
OXIDES
OXYGEN COMPOUNDS
PIGMENTS
SPECTRA
550700* - Microbiology