Journal
ACS OMEGA
Volume 2, Issue 8, Pages 4180-4187Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsomega.7b00640
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Funding
- National Aeronautics and Space Administration Astrobiology: Exobiology and Evolutionary Biology Grant [NNX13AI05G]
- Virginia Tech Agricultural Experiment Station Hatch Program [VA-160021]
- NASA [NNX13AI05G, 473104] Funding Source: Federal RePORTER
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Flavin-containing Trx reductase (TrxR) of Thermoplasma acidophilum (Ta), a thermoacidophilic facultative anaerobic archaeon, lacks the structural features for the binding of 2'-phosphate of nicotinamide adenine dinucleotide phosphate (NADPH), and this feature has justified the observed lack of activity with NADPH; NADH has also been reported to be ineffective. Our recent phylogenetic analysis identified Ta-TrxR as closely related to the NADHdependent enzymes of Thermotoga maritima and Desulfovibrio vulgaris, both being anaerobic bacteria. This observation instigated a reexamination of the activity of the enzyme, which showed that Ta-TrxR is NADH dependent; the apparent Km for NADH was 3.1 mu M, a physiologically relevant value. This finding is consistent with the observation that NADH: TrxR has thus far been found primarily in anaerobic bacteria and archaea.
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