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1 t in the crystal structure of wild type (wt) deoxymyoglobin.
2 gen average distances close to the value for deoxymyoglobin (2.05 +/- 0.01 A), while the distance fro
3      All model compounds as well as those of deoxymyoglobin and deoxyhemoglobin, previously studied,
4 ron porphyrin; (5) ferrous high-spin (S = 2) deoxymyoglobin and deoxyhemoglobin; and (6) ferric high
5 the difference between the static spectra of deoxymyoglobin and MbNO, showing the formation of an int
6                      Indeed, the addition of deoxymyoglobin and nitrite to isolated rat heart and liv
7 e pHu beef showed lower lightness and higher deoxymyoglobin compared with normal pHu (P < 0.05).
8 ess (a*), colour stability, oxymyoglobin and deoxymyoglobin decreased, but metmyoglobin, TBARS, perox
9 ns at the E7 position (His64) of sperm whale deoxymyoglobin (deoxyMb) are used as a probe of distal p
10 nt distal heme pocket mutants of sperm whale deoxymyoglobin (deoxyMb) has been investigated.
11 uggest a vital role for deoxyhemoglobin- and deoxymyoglobin-dependent nitrite reduction.
12 ntaining diamagnetic analogue of sperm whale deoxymyoglobin has been measured as a function of oxygen
13 ate to the solvent from which they rebind to deoxymyoglobin in a bimolecular process with a second-or
14                        The binding of HNO to deoxymyoglobin is rapid and essentially irreversible, wh
15 ne (PCr)/ATP was determined with 31P NMR and deoxymyoglobin (Mb-delta) with 1H NMR in myocardium remo
16                                              Deoxymyoglobin (Mb-Fe(II)) rapidly reacts with HNO produ
17 P)Cl (S = (5)/(2)), Mn(TPP)Cl (S = 2), and a deoxymyoglobin model (S = 2).
18 is and characterization of six new high-spin deoxymyoglobin models (imidazole(tetraarylporphyrinato)i
19 a second order reaction that is dependent on deoxymyoglobin, nitrite and proton concentration, with a
20  chemiluminescent measurements show that the deoxymyoglobin-nitrite reaction produces NO in a second
21 ket, perhaps accompanying rehydration of the deoxymyoglobin photoproduct or accommodation of protein
22 ons of wild-type, H64Q, H64A, H64L, and V68F deoxymyoglobin, respectively.
23 mal structural decomposition of the hemes in deoxymyoglobins reveals a predominantly dom heme deforma
24 sodium nitrite to transform oxymyoglobin and deoxymyoglobin to the more stable metmyoglobin.
25 t O(2), and we have previously reported that deoxymyoglobin traps free HNO to form a stable adduct.
26          A more rapid reaction occurred when deoxymyoglobin was used, further supporting the observat
27 l histidine residue (13)C NMR assignments in deoxymyoglobin which are confirmed by new quantitative N
28 aracterize the nitrite reductase activity of deoxymyoglobin, which reduces nitrite approximately 36 t
29 -studied geminate recombination processes of deoxymyoglobin with O(2), CO, and NO.