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. 2020 Jun 17;11:1109. doi: 10.3389/fmicb.2020.01109

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Copyright © 2020 Losey, Poudel, Boyd and McInerney.

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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Comparison of subunit compositions and domains between S. aciditrophicus HydAB, S. wolfei Hyd1ABC, and N. ovalis [FeFe]-hydrogenases. Cofactor binding sites are orientated from the N-terminal to C-terminal portion of each subunit. Gray shading indicates subunits that are fused together into a single polypeptide chain. The number of total amino acid residues for each is displayed to the right and is marked with a star. The peptides and domains are not scaled proportionally to accurately reflect number of amino acids in each subunit.