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. 2018 Dec 17;9:3130. doi: 10.3389/fmicb.2018.03130

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Copyright © 2018 Gregson, Metodieva, Metodiev, Golyshin and McKew.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Spectral counts (means ± SE; n = 4) of differentially expressed terminal alkane oxidation proteins during growth on a medium-chain alkane (n-C₁₄,), a long-chain alkane (n-C₂₈,) and a non-hydrocarbon control (Tween 80) in Thalassolituus oleivorans MIL-1. ^∗ denotes spectral counts significantly greater (P < 0.05) during growth on n-C₁₄ relative to growth on n-C₂₈ and TW. (B) Oxidation of an n-alkane by the identified proteins in the non-heme iron alkane monooxygenase system. The ferredoxin reductase (FdxR) oxidizes NAD(P)H to NAD(P)⁺. The electrons (e^-) generated from this are shuttled to the alkane monooxygenase (AM) by the ferredoxin (Fdx). The monooxygenase introduces oxygen into the alkane at the terminal carbon converting it into a primary alcohol. This alcohol is further oxidized to an aldehyde and then to a fatty acid by the alcohol dehydrogenase (AD) and aldehyde dehydrogenase (ALD), respectively.