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Nicotinamide adenine dinucleotide is a crucial coenzyme in cellular metabolism and is implicated in various diseases. This work introduces an electrochemical bioanalytical method utilizing solution-phase formate dehydrogenase (CbFDH) for detecting its oxidized form (NAD) in human blood plasma samples. The detection mechanism involves the catalytic conversion of NAD to NADH, facilitated by CbFDH in the presence of formate.

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Background: Programmed cell death plays an important role in neuronal injury and death after ischemic stroke (IS), leading to cellular glucose deficiency. Glucose deficiency can cause abnormal accumulation of cytotoxic disulfides, resulting in disulfidptosis. Ferroptosis, apoptosis, necroptosis, and autophagy inhibitors cannot inhibit this novel programmed cell death mechanism.

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Characterization of the oxygen-tolerant formate dehydrogenase from .

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Department of Plant Physiology, Institute of Biosciences, University of Rostock, Rostock, Germany.

Fixation of CO into the organic compound formate by formate dehydrogenases (FDHs) is regarded as the oldest autotrophic process on Earth. It has been proposed that an FDH-dependent CO fixation module could support CO assimilation even in photoautotrophic organisms. In the present study, we characterized FDH from (FDH) due to its ability to reduce CO under aerobic conditions.

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