n-Octane is used in organic syntheses, calibrations, and azeotropic distillations and is a common component of gasoline and other petroleum products. The engine fuel antiknocking properties of an isomer of n-octane (2,2,4-trimethylpentane or isooctane) are used as a comparative standard in the Octane Rating System. Many microorganisms, including several Pseudomonads, are able to use linear alkanes as their sole source of carbon and energy ([http://www.ncbi.nlm.nih.gov/pubmed/7532480|Beilen et al., 1994]). The OCT-plasmid of Pseudomonas oleovorans contains two operons, alkBFGHJKL and alkST, which encode all proteins necessary for the degradation of n-octane and other five- to twelve-carbon linear alkanes ([http://www.ncbi.nlm.nih.gov/pubmed/7532480|Beilen et al., 1994]). Branched isomers, such as isooctane, are less susceptible to biodegradation than n-octane ([http://www.ncbi.nlm.nih.gov/pubmed/539824|Schaeffer et al., 1979]). The conversion of n-octane to 1-octanol is catalyzed by a group of proteins collectively referred to as the "alkane hydroxylase system." It has three main components: alkane 1-monooxygenase, and the two soluble proteins rubredoxin, and rubredoxin reductase. Rubredoxin reductase transfers electrons from NADH to rubredoxin. This protein then passes electrons to alkane 1-monoxygenase, an enzyme localized in the cytoplasmic membrane. The final product of this pathway, octanoyl-CoA, enters the beta-oxidation cycle and is used as both a carbon and energy source ([http://www.ncbi.nlm.nih.gov/pubmed/7532480|Beilen et al., 1994]). The alkyl hydroperoxide reductase enzyme system of Salmonella choleraesuis (formerly S. typhimurium) is composed of two enzymes (AhpC and AhpF) which reduce organic hydroperoxides and hydrogen peroxide ([http://www.ncbi.nlm.nih.gov/pubmed/8555199|Poole 1996]. Homologs of these enzymes are found in a variety of Gram-positive and Gram-negative species.