https://doi.org/10.5061/dryad.00000008r

The kinetics data are stored in Excel files and the filenames correspond to the figures in "Mechanism of stepwise electron transfer in six-transmembrane epithelial antigen of the prostate (STEAP) 1 and 2" by Kehan Chen, Lie Wang, Jiemin Shen, Ah-lim Tsai, Ming Zhou and Gang Wu, https://doi.org/10.7554/eLife.88299.1. In each data file, the title of each sheet indicates the panel in the figure and the reaction.

The structures of different types of kinetic data are described as follows.

1. Time-dependent spectral change (Figure2, Figure2-FigureSupplement1, Figure3, Figure3-FigureSupplement1, Figure4-FigureSupplement1) The first column is the wavelength and the spectra are listed continuously from column 2. The spectrum acquired at the first time point is always in column 2 and marked "spectrum#1" in the top, and the temporal sequence of the spectra are marked in the top of each column. The acquisition time points of the spectra are listed in the two columns following the last spectrum.
2. Time courses of the Soret absorbance of ferrous heme (Figure3-FigureSupplement1, Figure5) The data is presented in two columns, the left one is the time points (in second) and the right is the absorbance at 427 nm (A₄₂₇).
3. Rate-dependence on the concentration of reduced FADH₂ or ferric.NTA (Figure2, Figure2-FigureSupplement1, Figure5) The left column is the concentration of reduced FAD (FADH₂) (in uM) or ferric.NTA (Fe³⁺.NTA) (in uM), followed by the columns of the rate constants, k_obs (in s^-1) of the fast phase, k_obs_1 and the slow phase, k_obs_2.
4. Bio-layer Interferometry (Figure3-FigureSupplement2). The profiles of association and dissociation are labeled with the concentration cytochrome b₅ reductase (b₅R) in the top and the response (Red) is listed versus the concentration of b₅R (in uM).

The data sheets in each file are listed below.
1. Figure 2
a. "PanelA STEAP1+FADH2": the spectral change during the reaction of STEAP1 with reduced FAD (FADH₂); Panel A in Figure 2.
b. "PanelBkobs(STEAP1+FADH2)vsFADH2": the dependence of the rate constants, k_obs in the reaction of STEAP1 with FADH₂, on the concentration of FADH₂; Panel B in Figure 2.
c. "PanelC STEAP1-STEAP2+NADPH": the spectral change in the reaction of the mixture of STEAP1 and STEAP2 with NADPH; Panel C in Figure 2.
2. Figure 2-FigureSupplement1
"PanelC L230GSTEAP1+FADH2": the spectral change in the reaction of STEAP1 Leu230Gly mutant with reduced FAD (FADH₂) and the dependence of rate constants, k_obs, on the concentration of FADH₂; Panel C in Figure 2-figuresupplement1.
3. Figure 3
a. "PanelA STEAP1-b5R+NADH": the spectral change in the reaction of STEAP1 plus cytochrome b₅ reductase (b₅R) with NADH; Panel A in Figure 3.
b. "PanelB L230GSTEAP1-b5R+NADH": the spectral change in the reaction of STEAP1 Leu230Gly mutant plus b₅R with NADH; Panel B in Figure 3.
4. Figure 3-FigureSupplement1
a. "PanelA": the time courses of A₄₂₇ in the reaction of STEAP1 only with NADPH and STEAP1 plus b₅R with NADH; Panel A in Figure 3-
figuresupplement1.
b. "PanelB" the spectral change in the reaction of STEAP1 plus FAD with NADPH; Panel B-figuresupplement1.
5. Figure 3-FigureSupplement2
"Sheet1": (1) the bio-layer interferometry profiles in the binding of b₅R to STEAP1; Panel A in Figure 3-figuresupplement2; (2) the dependence of
response on the concentration of b₅R; Panel B in Figure 3-figuresupplement2.
6. Figure 4-FigureSupplement1
a. "PanelA STEAP2+NADPH": the spectral change in the reaction of STEAP2 plus FAD with NADPH; Panel A in Figure 4-figuresupplement1.
b. "PanelB STEAP2+FADH2": the spectral change in the reaction of STEAP2 with reduced FAD (FADH₂); Panel B in Figure 4-figuresupplement1.
7. Figure 5
a. "PanelA&B STEAP1+Fe.NTA": (1) the time courses of A₄₂₇ in the reaction of ferrous STEAP1 with Fe³⁺.NTA; Panel A in Figure 5; (2) the
dependence of the rate constants, k_obs, on the concentration of Fe³⁺.NTA; Panel B in Figure 5.
b. "PanelC&D STEAP2+Fe.NTA": (1) the time courses of A₄₂₇ in the reaction of ferrous STEAP2 with Fe³⁺.NTA; Panel C in Figure 5; (2) the
dependence of the rate constants, k_obs, on the concentration of Fe³⁺.NTA; Panel D in Figure 5.