(A) The apo-protein is reconstituted with the ferric heme b to yield a corresponding 5-coordinated heme species. The arrows indicate the direction of change in absorbance intensity with the addition of ferric heme-b. (B) The absorbance at 410 nm is plotted against Molar ratio of [heme]/[apo-C14AM69A], showing a saturation of the Soret band.</p
<p>Following protein-ligand reconstitution and removal of unbound carotenoid the absorbance spectrum...
<p>A and C: UV-visible spectra of apo-FepB (gray line) and FepB-hemin or FepB-PPIX complex of 2.2 mM...
Apomyoglobin is obtained from pure myoglobin by extracting out the heme group. UsingUV-visible spect...
<p>(A, B) Holo-cyt. b<sub>6</sub> was proteolytically digested with proteinase K. At defined time po...
<p>(<b>A</b>) Comparison of the absorption spectrum of 3.2 µM holoShr alone with the spectrum of a m...
<p>(<b>A</b>) Comparison of the spectrum of holoShr, holoShp, and metHb. (<b>B–D</b>) The sum of the...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
Heme proteins are highly versatile with important roles in biochemistry including oxygen tra...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
(A) 5 μM of apo-protein was mixed with one equivalent simple PPIX. The arrows indicate the direction...
Much information about the heme-binding groups of hemoproteins have been obtained from model studies...
<p>(A) Proteins were separated on an 18% SDS gel. M: molecular mass standard; P: cell-free expressed...
AbstractApo-myoglobin covalently linked on CNBr-activated Sepharose 4B is proposed as a new heme acc...
The X−ray crystallographic analysis of redox−active systems may be complicated by photoreduction. Al...
<p>Following protein-ligand reconstitution and removal of unbound carotenoid the absorbance spectrum...
<p>A and C: UV-visible spectra of apo-FepB (gray line) and FepB-hemin or FepB-PPIX complex of 2.2 mM...
Apomyoglobin is obtained from pure myoglobin by extracting out the heme group. UsingUV-visible spect...
<p>(A, B) Holo-cyt. b<sub>6</sub> was proteolytically digested with proteinase K. At defined time po...
<p>(<b>A</b>) Comparison of the absorption spectrum of 3.2 µM holoShr alone with the spectrum of a m...
<p>(<b>A</b>) Comparison of the spectrum of holoShr, holoShp, and metHb. (<b>B–D</b>) The sum of the...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
Heme proteins are highly versatile with important roles in biochemistry including oxygen tra...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
20 mM Tris-HCl, pH 8.0, and 0.45 M sucrose, and absorbance time courses at 425 and 405 or 410 nm wer...
(A) 5 μM of apo-protein was mixed with one equivalent simple PPIX. The arrows indicate the direction...
Much information about the heme-binding groups of hemoproteins have been obtained from model studies...
<p>(A) Proteins were separated on an 18% SDS gel. M: molecular mass standard; P: cell-free expressed...
AbstractApo-myoglobin covalently linked on CNBr-activated Sepharose 4B is proposed as a new heme acc...
The X−ray crystallographic analysis of redox−active systems may be complicated by photoreduction. Al...
<p>Following protein-ligand reconstitution and removal of unbound carotenoid the absorbance spectrum...
<p>A and C: UV-visible spectra of apo-FepB (gray line) and FepB-hemin or FepB-PPIX complex of 2.2 mM...
Apomyoglobin is obtained from pure myoglobin by extracting out the heme group. UsingUV-visible spect...