Kinetics of ligand binding of cytochrome oxidases: a comparative study.
The plethora of microbial oxidases revealed by photochemical action spectra (Chance, B. (1989)) Biochim. Biophys. Acta 1000, 345-347) has led to detailed identification, purification and overproduction in many species, to the point where kinetic comparison of properties seems to allow structure/function deductions. This work compares the carbon monoxide recombination of five types of oxidases obtained from various organisms. The results are plotted in an Arrhenius-type plot and suggest that the carbon monoxide ligation is a sensitive indicator of the heme environment specific for an oxidase expressed under a given oxygen concentration. This survey of the carbon monoxide recombination kinetics of naturally occurring cytochrome oxidases in whole cells shows evidence for structural control of the reaction kinetics.
Basu
A
A
Wistar Institute, Philadelphia, PA 19104.
Yin
M
M
Waterland
R A
RA
Chance
B
B
D000818:Animals; D001419:Bacteria / Q000201:enzymology; D002248:Carbon Monoxide / Q000378:metabolism*; D002417:Cattle; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D009206:Myocardium / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013045:Species Specificity; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D008024:Ligands; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV