Over 100 distinct alkane monooxygenase (AlkB) enzymes containing a covalently bound, or fused, rubredoxin domain were identified and analyzed using bioinformatic techniques. One such protein was cloned as a full-length protein and truncated with its rubredoxin domain deleted. Its catalytic activity was evaluated, and its interaction with exogenous electron transfer partners was examined. These experiments shed light on the diversity of AlkB structure and reactivity, and the interaction of AlkBs with electron transfer partners.