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. 2016 Oct 4;7(1):10.1128/ecosalplus.ESP-0011-2016. doi: 10.1128/ecosalplus.esp-0011-2016

Table 1.

Comparison of the properties of the hydrogenase isoenzymes

Enzyme Subunit composition/electron pathway Metals and cofactors Function Dye specificity App. Km for H2 References
Hydrogenase-1 α2β2γ2 (HyaB-HyaA-HyaC)2 [NiFe]; [4Fe-3S], [3Fe-4S], [4Fe-4S]; cyt b H2 oxidation, O2 tolerance Nitroblue tetrazolium, Benzyl viologen (BV) 9 μM (PFEa)2 μM (BV) (141, 154, 156)
Hydrogenase-2 αβγδ (HybC-HybO-HybA-HybB) [NiFe]; 2 [4Fe-4S], [3Fe-4S]; 4 [FeS] H2 oxidation, energy conservation Benzyl viologen 17 μM (PFE)3.7 μM (BV) (13, 144, 154, 158)
Hydrogenase-3 (FHL complex) FdhH–HycB-G–HycE Mo-bis-PGD,b Selenocysteine, [4Fe-4S]; 7 [4Fe-4S]; [NiFe] Proton reduction Benzyl viologen 34 μM (PFE) (28, 29)
Hydrogenase-4 (E. coli) ?–HyfA-I predicted FHL ortholog Proton reduction? Unknown Unknown (7)
Hydrogenase-5 (Salmonella Typhimurium) α2β2γ2 (HydB-HydA-HydC)2 [NiFe]; [4Fe-3S], [3Fe-4S], [4Fe-4S]; cyt b H2 oxidation, O2 tolerance Nitroblue tetrazolium, Benzyl viologen 9 μM (PFE) (11, 12)
a

PFE, protein film electrochemistry.

b

Mo-bis-PGD, molybdopterin guanine dinucleotide.