PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1928719-5 1991 The rate of conversion from Fe3+ to the reduced Fe2+ in myoglobin, under given electrophoretic conditions, followed first-order kinetics with a rate constant at 30 degrees C of 304 s-1. ammonium ferrous sulfate 48-52 myoglobin Homo sapiens 56-65 1420896-2 1992 The stability properties of the iron(II)-dioxygen bond in myoglobin and hemoglobin are of particular importance, because both proteins are oxidized easily to the ferric met-form, which cannot be oxygenated and is therefore physiologically inactive. ammonium ferrous sulfate 32-40 myoglobin Homo sapiens 58-67 35599166-2 2022 Five key reactions of NO with mammalian muscle myoglobin (Mb) and red blood cell hemoglobin (Hb) have been examined: (1) reversible NO binding to Fe(II) forms; (2) reversible NO binding to Fe(III) forms; (3) NO dioxygenation by Fe(II)O2 complexes; (4) autoxidation of Fe(II)NO complexes in the presence of O2; and (5) autoreduction of Fe(III)NO complexes. ammonium ferrous sulfate 146-152 myoglobin Homo sapiens 47-56 35599166-2 2022 Five key reactions of NO with mammalian muscle myoglobin (Mb) and red blood cell hemoglobin (Hb) have been examined: (1) reversible NO binding to Fe(II) forms; (2) reversible NO binding to Fe(III) forms; (3) NO dioxygenation by Fe(II)O2 complexes; (4) autoxidation of Fe(II)NO complexes in the presence of O2; and (5) autoreduction of Fe(III)NO complexes. ammonium ferrous sulfate 268-274 myoglobin Homo sapiens 47-56 2792847-5 1989 Iron(II) complexes such as haemin from the breakdown of dietary haemoglobin and myoglobin also serve as growth factors for these bacteria and provide a rich source of haem-iron for intestinal uptake. ammonium ferrous sulfate 0-8 myoglobin Homo sapiens 80-89 25955505-6 2015 The peaks were attributed to the redox couple of heme Fe(II)/Fe(III) of the well-oriented Mb in Brij 56 matrix. ammonium ferrous sulfate 54-60 myoglobin Homo sapiens 90-92 27019153-4 2016 Mb-SGO-Nafion film modified electrode showed a pair of well-defined and nearly reversible cyclic voltammetry peaks at around -0.39 V versus saturated calomel electrode (SCE) in pH 7.0 buffers, characteristic of heme Fe(III)/Fe(II) redox couples. ammonium ferrous sulfate 224-230 myoglobin Homo sapiens 0-2 20232815-5 2010 Analysis of the ac harmonics, and with the hypothesis that the Fe(II)/Fe(I) process reflects the myoglobin state, suggests that the majority of the iron heme is released from myoglobin-DDAB (pH 5.0, no NaBr) films in contact with pH 5.0 (0.1 M sodium acetate) buffer solution devoid of or containing NaBr. ammonium ferrous sulfate 63-69 myoglobin Homo sapiens 175-184 23608540-5 2013 The electrode displayed a pair of quasi-reversible reduction-oxidation peaks at -0.3 and -0.2V, respectively, due to the Mb [Fe(3+)/Fe(2+)] redox couple, which is a surface-controlled electrochemical process with one electron transfer. ammonium ferrous sulfate 132-138 myoglobin Homo sapiens 121-123 20568729-1 2010 Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. ammonium ferrous sulfate 240-247 myoglobin Homo sapiens 61-70 20568729-1 2010 Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. ammonium ferrous sulfate 240-247 myoglobin Homo sapiens 72-74 20232815-15 2010 In summary, higher harmonic ac voltammetric data indicate that the Fe(II)/Fe(I) process but not the Fe(III)/Fe(II) reflects the state of myoglobin in DDAB films. ammonium ferrous sulfate 67-73 myoglobin Homo sapiens 137-146 25578484-1 2015 Myoglobin (Mb) and hemoglobin have the biological ability to carry/store oxygen (O2), a property which requires its heme iron atom to be in the ferrous--Fe(II)--state. ammonium ferrous sulfate 153-159 myoglobin Homo sapiens 0-9 20303500-4 2010 A pair of well-defined redox peaks appeared on the cyclic voltammogram in pH 7.0 phosphate buffer solution (PBS) with the formal peak potential (E(0")) at -0.256 V (versus SCE), which was the typical electrochemical behavior of Mb heme Fe(III)/Fe(II) redox couples. ammonium ferrous sulfate 244-250 myoglobin Homo sapiens 228-230 20232815-6 2010 However, myoglobin films prepared with pH 5.0 buffer containing NaBr shows significant difference in the higher harmonic shapes and midpoint potentials in the Fe(II)/Fe(I) process relative to the case when heme molecules are used, although as noted in other studies, a significant fraction of the Mb is rendered electroinactive in the presence of NaBr. ammonium ferrous sulfate 159-165 myoglobin Homo sapiens 9-18 18616316-2 2008 The {HECE/AA}n-Mb films showed a nearly reversible cyclic voltammetric (CV) peak pair at about -0.34 V vs SCE in pH 7.0 buffers for Mb heme Fe(III)/Fe(II) redox couple, and the surface concentration of electroactive Mb in the films (Gamma*) was affected significantly by the pH of Mb loading solution and testing solution. ammonium ferrous sulfate 148-154 myoglobin Homo sapiens 15-17 19394899-4 2009 Cyclic voltammetric results showed that a pair of well-defined quasi-reversible redox peaks appeared in the pH 7.0 phosphate buffer solution (PBS), which was attributed to the direct electron transfer of Mb heme Fe(III)/Fe(II) redox couples with the modified electrode. ammonium ferrous sulfate 220-226 myoglobin Homo sapiens 204-206 19437988-3 2009 The Mb-loaded films at pyrolytic graphite (PG) electrodes, designated as {PA/ZrO2}n-Mb, demonstrated well-defined and quasi-reversible CV responses for Mb Fe(III)/Fe(II) redox couple and good electrocatalytic properties toward oxygen and H2O2. ammonium ferrous sulfate 163-169 myoglobin Homo sapiens 4-6 19437988-3 2009 The Mb-loaded films at pyrolytic graphite (PG) electrodes, designated as {PA/ZrO2}n-Mb, demonstrated well-defined and quasi-reversible CV responses for Mb Fe(III)/Fe(II) redox couple and good electrocatalytic properties toward oxygen and H2O2. ammonium ferrous sulfate 163-169 myoglobin Homo sapiens 84-86 19437988-3 2009 The Mb-loaded films at pyrolytic graphite (PG) electrodes, designated as {PA/ZrO2}n-Mb, demonstrated well-defined and quasi-reversible CV responses for Mb Fe(III)/Fe(II) redox couple and good electrocatalytic properties toward oxygen and H2O2. ammonium ferrous sulfate 163-169 myoglobin Homo sapiens 84-86 17561388-4 2007 {PPI-Au/Mb}(n) films on PG electrodes demonstrated a pair of well-defined and quasi-reversible CV reduction-oxidation peaks for Mb heme Fe(III)/Fe(II) couple and good electrocatalytic properties toward reduction of oxygen and hydrogen peroxide. ammonium ferrous sulfate 144-150 myoglobin Homo sapiens 8-10 21817623-4 2008 The loading behavior of {PDDA/SiO(2)}(n) films toward Mb was investigated by monitoring the cyclic voltammetric responses of the Mb heme Fe(III)/Fe(II) redox couple, and comparing them with those of {PDDA/PSS}(n) films, where PSS stands for poly(styrenesulfonate). ammonium ferrous sulfate 145-151 myoglobin Homo sapiens 54-56 17561388-4 2007 {PPI-Au/Mb}(n) films on PG electrodes demonstrated a pair of well-defined and quasi-reversible CV reduction-oxidation peaks for Mb heme Fe(III)/Fe(II) couple and good electrocatalytic properties toward reduction of oxygen and hydrogen peroxide. ammonium ferrous sulfate 144-150 myoglobin Homo sapiens 128-130 16331725-2 2006 Positive and negative ions are formed from solution myoglobin with Fe(2+) (ferromyoglobin) and Fe(3+) (ferrimyoglobin). ammonium ferrous sulfate 67-73 myoglobin Homo sapiens 52-61 16854161-2 2006 The Mb in {Mb/HA}(n) films showed a quasi-reversible cyclic voltammetry (CV) response for its heme Fe(III)/Fe(II) redox couple. ammonium ferrous sulfate 107-113 myoglobin Homo sapiens 4-6 16854161-2 2006 The Mb in {Mb/HA}(n) films showed a quasi-reversible cyclic voltammetry (CV) response for its heme Fe(III)/Fe(II) redox couple. ammonium ferrous sulfate 107-113 myoglobin Homo sapiens 11-13 15803717-2 2004 Mb/sol-gel film modified electrodes show a pair of well-defined and nearly reversible cyclic voltammetric peaks for the Mb Fe(III)/Fe(II) redox couple at about -0.298 V (vs Ag/AgCl) in a pH 7.0 phosphate buffer solution. ammonium ferrous sulfate 131-137 myoglobin Homo sapiens 0-2 15301945-3 2004 Two couples of redox peaks corresponding to Fe(III) to Fe(II) conversion of the Mb intercalated in the mesopores and adsorbed on the surface of the HMS were observed with the formal potentials of -0.167 and -0.029V in 0.1M, pH 7.0, phosphate buffer solution, respectively. ammonium ferrous sulfate 55-61 myoglobin Homo sapiens 80-82 15112219-8 2004 The observed kinetics are in agreement with a reaction mechanism in which the nitric oxide that is initially bound to the Fe(II) centre of myoglobin is displaced by oxygen in a reversible ligand-exchange reaction prior to an irreversible electron transfer. ammonium ferrous sulfate 122-128 myoglobin Homo sapiens 139-148 15803717-2 2004 Mb/sol-gel film modified electrodes show a pair of well-defined and nearly reversible cyclic voltammetric peaks for the Mb Fe(III)/Fe(II) redox couple at about -0.298 V (vs Ag/AgCl) in a pH 7.0 phosphate buffer solution. ammonium ferrous sulfate 131-137 myoglobin Homo sapiens 120-122 15803717-3 2004 The formal potential of the Mb heme Fe(III)/Fe(II) couple shifted linearly with pH with a slope of 52.4 mV/pH, denoting that an electron transfer accompanies single-proton transportation. ammonium ferrous sulfate 44-50 myoglobin Homo sapiens 28-30 9108688-1 1997 Myoglobin (Mb) in thin films of phosphatidyl cholines (PC) or dihexadecyl phosphate (DHP) gave direct, reversible electron transfer between pyrolytic graphite electrodes and the heme Fe(III)/Fe(II) redox couple of the protein. ammonium ferrous sulfate 191-197 myoglobin Homo sapiens 0-9 12702396-3 2002 [AQ/Mb](n) films grown on pyrolytic graphite (PG) electrodes showed a pair of well-defined and nearly reversible CV peaks at about -0.20 V vs Ag/AgCl in pH 5.5 buffers, characteristic of the Mb heme Fe(III)/Fe(II) redox couple. ammonium ferrous sulfate 207-213 myoglobin Homo sapiens 4-6 11254342-3 2001 Incorporated myoglobin (Mb) in DHP-PDDA films on pyrolytic graphite (PG) electrodes showed a pair of well-defined and nearly reversible cyclic voltammetric peaks for the Mb Fe(III)/Fe(II) couple at about -0.3 V vs SCE in pH 7.0 buffers. ammonium ferrous sulfate 181-187 myoglobin Homo sapiens 13-22 11254342-3 2001 Incorporated myoglobin (Mb) in DHP-PDDA films on pyrolytic graphite (PG) electrodes showed a pair of well-defined and nearly reversible cyclic voltammetric peaks for the Mb Fe(III)/Fe(II) couple at about -0.3 V vs SCE in pH 7.0 buffers. ammonium ferrous sulfate 181-187 myoglobin Homo sapiens 24-26 14642907-2 2003 In pH 7.0 buffers, Mb and Hb incorporated in CMC films gave a pair of well-defined and quasi-reversible cyclic voltammetric peaks at about -0.34 V vs. SCE, respectively, characteristic of heme Fe(III)/Fe(II) redox couples of the proteins. ammonium ferrous sulfate 201-207 myoglobin Homo sapiens 19-21 18968594-2 2002 Mb-PAM film electrodes showed a pair of well-defined and nearly reversible cyclic voltammetric peaks for Mb Fe(III)/Fe(II) redox couple at about -0.27 (vs. SCE) in pH 5.5 buffers. ammonium ferrous sulfate 116-122 myoglobin Homo sapiens 0-2 18968594-2 2002 Mb-PAM film electrodes showed a pair of well-defined and nearly reversible cyclic voltammetric peaks for Mb Fe(III)/Fe(II) redox couple at about -0.27 (vs. SCE) in pH 5.5 buffers. ammonium ferrous sulfate 116-122 myoglobin Homo sapiens 105-107