Extended Data Fig. 1: Organization of the components of the AlkBGT biocatalysts.
From: Structural basis for enzymatic terminal C–H bond functionalization of alkanes
The three components (AlkB, AlkG, and AlkT) in the alkane hydroxylation biocatalyst are encoded as separate genes in P. oleovorans. AlkG is an Fe-sulfur cluster-containing redox protein that transfers electrons to the diiron center in AlkB. AlkT is a flavin adenine dinucleotide (FAD)-dependent rubredoxin reductase that transfers two electrons from NADH singly to the Fe-sulfur cluster of AlkG, which then relays two of them singly to AlkB to enable biocatalysis10,12. The membrane-bound AlkB is a nonheme diiron-containing monooxygenase that specifically oxidizes the terminal methyl group of alkanes to produce the corresponding primary alcohols8,10,13,14,17,22,30. There are microbes that have evolved to have the AlkB and AlkG fused together, presumably for improved electron transfer15,26. Additionally, in some species (Leptospira, Limnobacter, and Polaromonas), AlkB is fused with multiples proteins of an N-terminal ferredoxin and a ferredoxin reductase15.
