Data from: Formate dehydrogenase: The role of the AMP cofactor fragment in stabilization of the transition state for enzyme-catalyzed hydride transfer
Data files
Jun 18, 2026 version files 7.91 KB
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Data_FIgure_2A.csv
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Data_Figure_2B.csv
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Data_Figure_3.csv
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Data_Figure_S1.csv
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Data_Figure_S2.csv
180 B
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Data_Figure_S3.csv
178 B
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Data_Figure_S4.csv
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Data_Figure_S5.csv
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Data_Figure_S6.csv
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Data_Figure_S7.csv
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Figure_1.txt
559 B
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README.md
5.64 KB
Abstract
This paper reports: (1) A comparison of the inhibition constant Ki for azide ion inhibition of hydride transfer from formate to nicotinamide adenine dinucleotide (NAD) and for hydride transfer from formate to the truncated nucleoside nicotinamide riboside. (2) The effect of increasing concentrations of the truncated adenosine monophosphate (AMP) fragment on the inhibition constant Ki azide ion inhibition of hydride transfer from formate to NR.
Dataset DOI: 10.5061/dryad.79cnp5jbx
Description of the data and file structure
Data sets listed for several types or experiments.
Figure 1
Figure 1 reports initial velocities for formate dehydrogenase (FDH)-catalyzed hydride transfer from formate to nicotinamide adenine dinucleotide (NAD) determined at increasing concentrations of formate and at different fixed concentrations of the azide anion inhibitor. The variables for this plot are (1) v/[E] with units of reciprocal sec, where v is the velocity for enzyme-catalyzed hydride transfer from formate [HCOOH] to NAD and [E] is the concentration of FDH (M).
File: Figure_1.txt
Description: The effect of increasing [HCOOH] (M) on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to NAD for reactions at [NAD] = 1.3 mM and different fixed concentrations of azide ion. The data are fit to a model for competitive inhibition of FDH by azide anion to give a value of Ki (M) for inhibition by azide anion.
Variables
- [Formate] mM
- 0 mM az 1.0E-6 M az 3.0E-6 M az 5.0E-6 M az 7.0E-6 M az. 9.0E-6 M az. 1.0E-5 M az
Figure S1
Figure S1 reports initial reaction velocities v/[E] for FDH-catalyzed hydride transfer from formate [F] to nicotinamide riboside [NR] determined at increasing [NR][F]. The variables for this plot are (1) v/[E] with units of reciprocal sec, where v is the velocity for enzyme-catalyzed hydride transfer from formate to NR, and [E] is the concentration of FDH (M). (2) The product of the formate and NR reactant concentrations - [F][NR] with units of M2.
File: Data_Figure_S1.csv
Description: The effect of increasing [NRC][HCOOH]/M2 on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR].
Variables
- [NRC][HCOOH]/M2
- v/[E] (s-1)
Figures 2A, 2B, S2, S3, S4, S5, S6 and S7
Figures 2A, 2B, S2, S3, S4, S5, S6 and S7 report initial velocities v/[E] for FDH-catalyzed hydride transfer from formate to nicotinamide riboside [NR] at different fixed concentrations of adenosine 5'-monophosphate [AMP]. The variables for these plots are v/[E] with units of reciprocal sec, where v is the velocity for enzyme-catalyzed hydride transfer from formate to NR, and [E] is the concentration of FDH. (2) The concentration of azide anion inhibitor. The data for each plot were fit to a Scheme for competitive inhibition by azide anion to give inhibition constants Ki for reactions carried out at the different [AMP].
File: Data_FIgure_2A.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 0 M. No data is reported for the reaction at [az] = 5 mM.
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_2B.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 10 mM.
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_S2.csv
Description: Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 0.10mM
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_S3.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 0.20mM
Variables
- [Azide] mM
- v/E (s-1)
File: Data_Figure_S4.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 0.40mM
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_S5.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 0.80mM
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_S6.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 1.0 mM
Variables
- [Azide] mM
- v/[E] (s-1)
File: Data_Figure_S7.csv
Description: The effect of increasing [az] on the initial velocity for FDH-catalyzed hydride transfer from formate [HCOOH] to nicotinamide riboside [NR] and at [AMP] = 5.0 mM.
Variables
- [Azide] mM
- v/[E] (s-1)
Figure 3
Figure 3 shows the effect of increasing [AMP] on Ki for inhibition by azide ion. The variables for this plot are: (1) The inhibition constant K1 (mM) for reactions at the given concentration of [AMP]. (2) The concentration of the azide ion inhibitor (mM).
Notes on variables: All values of v/[E] have units of s-1. Reactant and inhibitor concentrations have units of mM (0.001 M) unless noted otherwise. The enzyme concentration has units of M. Inhibition constants Ki have units of mM.
File: Data_Figure_3.csv
Description: Description: The effect of increasing [AMP] (mM) on the inhibition constant Ki (mM) for inhibition of FDH-catalyzed hydride transfer from formate to NR by azide anion.
Variables
- [AMP] (mM)
- Ki (N3-)/mM
The progress of hydride transfer from formate to NAD or NR was monitored by following the increase in absorbance the the reduced NADH cofactor or NRH cofactor fragment.