<p>(<b>A</b>) Comparison of the absorption spectrum of 3.2 µM holoShr alone with the spectrum of a mixture of 3.2 µM holoShr and 23 µM apoShp. The spectrum of the mixture was taken immediately after mixing, and the spectrum of 3.2 µM holoShp was included for comparison. (<b>B</b>) ApoShp titration in heme transfer from holoShr to apoShp. Shown are the A<sub>280</sub>/A<sub>408</sub> ratio of the recovered Shr and the amount of transferred heme.</p
<p>(<b>A</b>) Shr enhances the rate of heme transfer from metHb to apoShp. (<b>B</b>) Enhancement of...
The absorption spectrum of reduced H-450 was reversibly affected by a pH cnange; the Soret peak of t...
<p>Both spectra were recorded at 25°C in 10 mM Tris-HCl buffer, pH 7.4. The concentrations of HSA an...
<p>(<b>A</b>) Spectral shift in heme transfer from holoHtsA to apoShp. Absorption spectra of 1.3 µM ...
<p>(<b>A</b>) Spectral shift in heme transfer from holoShr to apoShp. Absorption spectra of 0.8 µM h...
<p>(<b>A</b>) Comparison of the spectrum of holoShr, holoShp, and metHb. (<b>B–D</b>) The sum of the...
<p>(<b>A</b>) Absorption spectrum of Hb before and after the reaction of metHb with apoShr. (<b>B</b...
<p>(A) Overlay of the absorption spectra of holo-NS-N1-MD-N<sup>IsdC</sup> and holo-IsdC. (B) No shi...
<p>(A) Absorption spectrum comparison of metHb (3 µM heme), metHb (3 µM heme)/30 µM apo-N2, and 3 µM...
<p>(A) No shift in the spectrum of a mixture of 3.0 µM metHb heme and 30 µM apo-N2 at the indicated ...
(A) The apo-protein is reconstituted with the ferric heme b to yield a corresponding 5-coordinated h...
<p>Spectral traces were recorded after 2 h of incubation of a fixed amount (1.5 µM) of LPO-Fe(III) (...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
<p>Spectrum of OxyHb (5 µM) was recorded. H<sub>2</sub>O<sub>2</sub> (to yield 6 µM) was added and t...
<p>(<b>A</b>) Shr enhances the rate of heme transfer from metHb to apoShp. (<b>B</b>) Enhancement of...
The absorption spectrum of reduced H-450 was reversibly affected by a pH cnange; the Soret peak of t...
<p>Both spectra were recorded at 25°C in 10 mM Tris-HCl buffer, pH 7.4. The concentrations of HSA an...
<p>(<b>A</b>) Spectral shift in heme transfer from holoHtsA to apoShp. Absorption spectra of 1.3 µM ...
<p>(<b>A</b>) Spectral shift in heme transfer from holoShr to apoShp. Absorption spectra of 0.8 µM h...
<p>(<b>A</b>) Comparison of the spectrum of holoShr, holoShp, and metHb. (<b>B–D</b>) The sum of the...
<p>(<b>A</b>) Absorption spectrum of Hb before and after the reaction of metHb with apoShr. (<b>B</b...
<p>(A) Overlay of the absorption spectra of holo-NS-N1-MD-N<sup>IsdC</sup> and holo-IsdC. (B) No shi...
<p>(A) Absorption spectrum comparison of metHb (3 µM heme), metHb (3 µM heme)/30 µM apo-N2, and 3 µM...
<p>(A) No shift in the spectrum of a mixture of 3.0 µM metHb heme and 30 µM apo-N2 at the indicated ...
(A) The apo-protein is reconstituted with the ferric heme b to yield a corresponding 5-coordinated h...
<p>Spectral traces were recorded after 2 h of incubation of a fixed amount (1.5 µM) of LPO-Fe(III) (...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
<p>Spectrum of OxyHb (5 µM) was recorded. H<sub>2</sub>O<sub>2</sub> (to yield 6 µM) was added and t...
<p>(<b>A</b>) Shr enhances the rate of heme transfer from metHb to apoShp. (<b>B</b>) Enhancement of...
The absorption spectrum of reduced H-450 was reversibly affected by a pH cnange; the Soret peak of t...
<p>Both spectra were recorded at 25°C in 10 mM Tris-HCl buffer, pH 7.4. The concentrations of HSA an...