1.8.7.3	744307	 A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis	Biochemistry	 46	 12875-12885 	2007	Methanothermobacter marburgensis	
1.8.7.3	743210	 A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea	mBio	 8	 e02285-16 	2017	Methanosarcina acetivorans	
1.8.7.3	745383	 Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate	 quinone reductase	J. Biol. Inorg. Chem.	 18	 905-915 	2013	Methanothermobacter marburgensis	
1.8.7.3	764753	 Electron bifurcation and confurcation in methanogenesis and reverse methanogenesis	Front. Microbiol.	 9	 1322 	2018	Methanothermococcus thermolithotrophicus	
1.8.7.3	764753	 Electron bifurcation and confurcation in methanogenesis and reverse methanogenesis	Front. Microbiol.	 9	 1322 	2018	Methanothermococcus thermolithotrophicus DSM 2095	
1.8.7.3	764472	 Electron bifurcation makes the puzzle pieces fall energetically into place in methanogenic energy conservation	ChemBioChem	 18	 2295-2297 	2017	Methanothermococcus thermolithotrophicus	
1.8.7.3	764472	 Electron bifurcation makes the puzzle pieces fall energetically into place in methanogenic energy conservation	ChemBioChem	 18	 2295-2297 	2017	Methanothermococcus thermolithotrophicus DSM 2095	
1.8.7.3	764654	 Energy conservation in the gut microbe Methanomassiliicoccus luminyensis is based on membrane-bound ferredoxin oxidation coupled to heterodisulfide reduction	FEBS J.	 286	 3831-3843 	2019	Methanomassiliicoccus luminyensis	
1.8.7.3	742500	 Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis	FEBS J.	 283	 472-483 	2016	Methanomassiliicoccus luminyensis	
1.8.7.3	742500	 Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis	FEBS J.	 283	 472-483 	2016	Methanomassiliicoccus luminyensis DSM 25720	
1.8.7.3	745797	 Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase	Mol. Microbiol.	 75	 843-853 	2010	Methanosarcina acetivorans	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanothermobacter wolfeii	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanothermococcus thermolithotrophicus	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii NBRC 100440	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii DSM 2661	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii ATCC 43067	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii JAL-1	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanothermococcus thermolithotrophicus DSM 2095	
1.8.7.3	765831	 Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction	Science	 357	 699-703 	2017	Methanocaldococcus jannaschii JCM 10045	
1.8.7.3	744972	 Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus	Front. Microbiol.	 10	 17 	2011	Acidithiobacillus caldus	
1.8.7.3	742382	 The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough	Environ. Microbiol.	 17	 2288-2305 	2015	Desulfovibrio vulgaris	
1.8.7.3	742382	 The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough	Environ. Microbiol.	 17	 2288-2305 	2015	Desulfovibrio vulgaris ATCC 29579	
1.8.7.3	765833	 Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes	Science	 373	 1151-1156 	2021	Methanospirillum hungatei