title: Kinetics of ligand binding of cytochrome oxidases: a comparative study.
abstract: 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.
authors.affiliation: Wistar Institute, Philadelphia, PA 19104.
authors.forename: A
authors.initials: A
authors.lastname: Basu
authors.forename: M
authors.initials: M
authors.lastname: Yin
authors.forename: R A
authors.initials: RA
authors.lastname: Waterland
authors.forename: B
authors.initials: B
authors.lastname: Chance
mesh_terms: 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
chemical_list: D008024:Ligands; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV