a<p>The data were obtained using 3 µM heme donor and 30 µM each component in heme acceptor mixtures unless specified otherwise. Percentages of heme transferred were obtained at 30 min of the fast metHb/IsdB, metHb/NS-N1-MD-N2, and metHb/N2/NS-N1-MD reactions and at 12 h of the other slower reactions.</p>b<p>40 µM H64Y/V68F Mb was used.</p>c<p>8 µM NS-N1-MD was used.</p
<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>) Spectral shift in heme transfer from holoShr to apoShp. Absorption spectra of 0.8 µM h...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...
<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<p>The halftime is defined as the amount of minutes for one-half of the heme to dissociate from Isd...
The rate constants for the association of oxygen and of carbon monoxide with reduced hemoglobin and ...
<p>(A) Rate determination for the formation of metHb (▪) and hemichromes (•) from hydrated samples. ...
<p>(B-F) Overlay of the experimental data (black curve) with curve(s) fit to a single or double expo...
<p>The rate of heme transfer to LDL was traced in reaction mixtures containing either Hb or Mb (3 µM...
<p>(A and B) Time courses of normalized ΔA<sub>600</sub> measuring heme dissociation from holo-N2 us...
Using the Förster equations we have estimated the rate of energy transfer from tryptophans to hemes ...
The development of two kinetic methods for quantitation of hemoglobin and methemoglobin is described...
<p>(A) Overlay of the absorption spectra of holo-NS-N1-MD-N<sup>IsdC</sup> and holo-IsdC. (B) No shi...
AbstractApo-myoglobin covalently linked on CNBr-activated Sepharose 4B is proposed as a new heme acc...
<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>) Spectral shift in heme transfer from holoShr to apoShp. Absorption spectra of 0.8 µM h...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...
<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<p>The halftime is defined as the amount of minutes for one-half of the heme to dissociate from Isd...
The rate constants for the association of oxygen and of carbon monoxide with reduced hemoglobin and ...
<p>(A) Rate determination for the formation of metHb (▪) and hemichromes (•) from hydrated samples. ...
<p>(B-F) Overlay of the experimental data (black curve) with curve(s) fit to a single or double expo...
<p>The rate of heme transfer to LDL was traced in reaction mixtures containing either Hb or Mb (3 µM...
<p>(A and B) Time courses of normalized ΔA<sub>600</sub> measuring heme dissociation from holo-N2 us...
Using the Förster equations we have estimated the rate of energy transfer from tryptophans to hemes ...
The development of two kinetic methods for quantitation of hemoglobin and methemoglobin is described...
<p>(A) Overlay of the absorption spectra of holo-NS-N1-MD-N<sup>IsdC</sup> and holo-IsdC. (B) No shi...
AbstractApo-myoglobin covalently linked on CNBr-activated Sepharose 4B is proposed as a new heme acc...
<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>) Spectral shift in heme transfer from holoShr to apoShp. Absorption spectra of 0.8 µM h...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...