Structure and reactivity of multiple forms of cytochrome oxidase as evaluated by x-ray absorption spectroscopy and kinetics of cyanide binding
0301 basic medicine
0303 health sciences
Binding Sites
Cyanides
Chemical Phenomena
Spectrometry, X-Ray Emission
Ferric Compounds
Electron Transport Complex IV
Chemistry
Kinetics
03 medical and health sciences
Animals
Cattle
Oxidation-Reduction
Copper
Sulfur
DOI:
10.1021/bi00320a051
Publication Date:
2005-03-08T07:50:16Z
AUTHORS (5)
ABSTRACT
The extended X-ray absorption fine structure (EXAFS) data show differences between the active site structures of different cytochrome oxidase preparations. In the resting (as isolated) state of the Yonetani preparation, the bridging atom between Fe3+a3 and Cu2+a3 is present [Powers, L., Chance, B., Ching, Y., & Angiolillo, P. (1981) Biophys. J. 34, 465], whereas in another preparation (e.g., Hartzell-Beinert), this atom seems to be bound only to Fe3+a3 in a significant fraction of the molecules. Both preparations bind cyanide in a multiphasic fashion, suggesting that the resting cytochrome oxidase is not homogeneous but rather is a mixture of several forms. The proportion of these forms as detected by cyanide binding kinetics differs for different preparations. However, upon reduction and reoxidation (conversion to the "oxygenated" form) the cyanide binding kinetics become monophasic and all preparations of the oxygenated form bind cyanide at the same rate. Thus, a combination of structural and kinetic approaches seems necessary for evaluation of the nature of the active site of cytochrome oxidase in its various forms.
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