Fig. 3: Genes inferred to be co-localized with those coding for methyl viologen-reducing (Group 3c) [NiFe]-hydrogenase (Mvh) and formate dehydrogenase (Fdh) in Type I and II MAGs (A) and the putative protein complexes they form to bifurcate electrons from H2 (B) or formate (C), respectively, to simultaneously reduce ferredoxin and heterodisulfide. | The ISME Journal

Fig. 3: Genes inferred to be co-localized with those coding for methyl viologen-reducing (Group 3c) [NiFe]-hydrogenase (Mvh) and formate dehydrogenase (Fdh) in Type I and II MAGs (A) and the putative protein complexes they form to bifurcate electrons from H2 (B) or formate (C), respectively, to simultaneously reduce ferredoxin and heterodisulfide.

From: Diversification of methanogens into hyperalkaline serpentinizing environments through adaptations to minimize oxidant limitation

Fig. 3

Percentages below each gene indicate amino acid identities between homologs encoded by Type I and Type II MAGs. In panels B and C, squares represent [4Fe-4S] clusters and triangles represent [2Fe-2S] clusters. CoB coenzyme B, CoM coenzyme M, FAD flavin adenine dinucleotide, Fd ferredoxin, Fdh formate dehydrogenase, Hdr heterodisulfide reductase, Mvh methyl viologen-reducing (Group 3c) hydrogenase. Figure modified from Thauer et al. [71] and Costa et al. [77].

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