PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9178424-0 1997 Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations. Deuterium 81-83 cytochrome c, somatic Homo sapiens 43-55 9324950-0 1997 Conformational properties of the A-state of cytochrome c studied by hydrogen/deuterium exchange and electrospray mass spectrometry. Deuterium 77-86 cytochrome c, somatic Homo sapiens 44-56 9377710-0 1997 Characterization of the free energy spectrum of peptostreptococcal protein L. BACKGROUND: Native state hydrogen/deuterium exchange studies on cytochrome c and RNase H revealed the presence of excited states with partially formed native structure. Deuterium 112-121 cytochrome c, somatic Homo sapiens 142-154 35326429-4 2022 In the cells, excessive amounts of H2S can potentially release cytochrome c protein from the mitochondria, increase the iron content of the cytosolic iron pool, and increase the amount of reactive oxygen species. Deuterium 35-38 cytochrome c, somatic Homo sapiens 63-75 7819193-0 1995 Tertiary stability of native and methionine-80 modified cytochrome c detected by proton-deuterium exchange using on-line Fourier transform infrared spectroscopy. Deuterium 88-97 cytochrome c, somatic Homo sapiens 56-68 8396450-1 1993 Deuterium and phosphorus nuclear magnetic resonance (NMR) has been used to investigate the dynamics of slow motional processes induced in bilayer cardiolipin upon binding with cytochrome c. Deuterium 0-9 cytochrome c, somatic Homo sapiens 176-188 1658332-2 1991 In high salt, acid cyt c (pD 2.2; where D is deuterium) is nearly as compact as the native form. Deuterium 45-54 cytochrome c, somatic Homo sapiens 19-24 1850290-9 1991 The interaction with cardiolipin bilayers appeared to create a high degree of mobility for the side-chain sites of [N epsilon, N epsilon-C2H3]lysyl cytochrome c and perturbed backbone structure to instantaneously release all deuterons in [amide-2H]cytochrome c. Deuterium 138-140 cytochrome c, somatic Homo sapiens 148-160 1850290-3 1991 Deuterium NMR has been used to investigate the structure and dynamic state of cytochrome c complexed with bilayers of cardiolipin. Deuterium 0-9 cytochrome c, somatic Homo sapiens 78-90 1850290-4 1991 Reductive methylation was employed to prepare [N epsilon, N epsilon-C2H3]lysyl cytochrome c, and deuterium exchange provided labeling of backbone sites to give [amide-2H]cytochrome c or more selective labeling of just histidine residues in [epsilon-2H]histidine cytochrome c. Deuterium 97-106 cytochrome c, somatic Homo sapiens 170-182 1850290-4 1991 Reductive methylation was employed to prepare [N epsilon, N epsilon-C2H3]lysyl cytochrome c, and deuterium exchange provided labeling of backbone sites to give [amide-2H]cytochrome c or more selective labeling of just histidine residues in [epsilon-2H]histidine cytochrome c. Deuterium 97-106 cytochrome c, somatic Homo sapiens 170-182 1850290-5 1991 Deuterium NMR measurements on [N epsilon, N epsilon-C2H3]lysyl cytochrome c in the solid state showed restricted motions, fairly typical of the behavior of aliphatic side-chain sites in proteins. Deuterium 0-9 cytochrome c, somatic Homo sapiens 63-75 1850290-6 1991 The [amide-2H]cytochrome c provided "immobile" amide spectra showing that only the most stable backbone sites remained labeled in this derivative. Deuterium 11-13 cytochrome c, somatic Homo sapiens 14-26 1850290-9 1991 The interaction with cardiolipin bilayers appeared to create a high degree of mobility for the side-chain sites of [N epsilon, N epsilon-C2H3]lysyl cytochrome c and perturbed backbone structure to instantaneously release all deuterons in [amide-2H]cytochrome c. Deuterium 225-234 cytochrome c, somatic Homo sapiens 148-160 2548599-8 1989 This band was used to show that Trp H/D exchange in D2O is much faster for FeIII than FeII cyt c. Deuterium 38-39 cytochrome c, somatic Homo sapiens 91-96 33441668-3 2021 In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Deuterium 111-120 cytochrome c, somatic Homo sapiens 57-62 166765-0 1975 [Influence of the oxidoreductive state on the kinetics of deuterium-hydrogen exchange in cytochrome c]. Deuterium 58-67 cytochrome c, somatic Homo sapiens 89-101 5666746-0 1968 Hydrogen-deuterium exchange of cytochrome c. Deuterium 9-18 cytochrome c, somatic Homo sapiens 31-43 5691140-0 1968 Hydrogen-deuterium exchange of cytochrome c. Deuterium 9-18 cytochrome c, somatic Homo sapiens 31-43 6297593-0 1983 Deuterium exchangeable proton hyperfine resonances of low-spin cytochrome c peroxidase and the mechanism of peroxidase catalysis. Deuterium 0-9 cytochrome c, somatic Homo sapiens 63-75 6297593-1 1983 Deuterium exchangeable hyperfine proton NMR resonances of cytochrome c peroxidase (EC 1.11.1.5) are identified in H2O solutions of the enzyme. Deuterium 0-9 cytochrome c, somatic Homo sapiens 58-70 18172-0 1977 H/2H isotope effect in redox reactions of cytochrome c. Deuterium 2-4 cytochrome c, somatic Homo sapiens 42-54 4625641-0 1972 [Study of the kinetics of hydrogen-deuterium exchange of cytochrome c at 20 and 38 degrees C]. Deuterium 35-44 cytochrome c, somatic Homo sapiens 57-69 33441668-4 2021 Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Deuterium 126-135 cytochrome c, somatic Homo sapiens 8-13 21959229-7 2012 Treatment of cells with EE-DS (80 mug/ml) for 48 h resulted in significant increase of cytochrome c in the cytosol, which indicated cytochrome c release from mitochondria. Deuterium 26-29 cytochrome c, somatic Homo sapiens 87-99 28742962-0 2017 Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics. Deuterium 79-88 cytochrome c, somatic Homo sapiens 51-63 28742962-2 2017 In the present work, the structural interrogation of kinetically trapped intermediates of cyt c was performed by correlating the ion-neutral collision cross section (CCS) and charge state with the starting solution conditions and time after desolvation using collision induced activation (CIA), time-resolved hydrogen/deuterium back exchange (HDX) and trapped ion mobility spectrometry-mass spectrometry (TIMS-MS). Deuterium 318-327 cytochrome c, somatic Homo sapiens 90-95 22746312-7 2012 Moreover, hydrogen/deuterium exchange (H/DX) combined with FTICR MS provides the sensitive method to insight the small conformation change of cytochrome c induced by cisplatin. Deuterium 19-28 cytochrome c, somatic Homo sapiens 142-154 21959229-7 2012 Treatment of cells with EE-DS (80 mug/ml) for 48 h resulted in significant increase of cytochrome c in the cytosol, which indicated cytochrome c release from mitochondria. Deuterium 26-29 cytochrome c, somatic Homo sapiens 132-144 19200750-1 2009 This work uses electrospray ionization mass spectrometry (ESI-MS) in conjunction with hydrogen/deuterium exchange (HDX) and optical spectroscopy for characterizing the solution-phase properties of cytochrome c (cyt c) after heat exposure. Deuterium 95-104 cytochrome c, somatic Homo sapiens 197-209 18371493-0 2008 Deuterium isotope effect of proton pumping in cytochrome c oxidase. Deuterium 0-9 cytochrome c, somatic Homo sapiens 46-58 15278784-0 2004 Solvent-based deuterium isotope effects on the redox thermodynamics of cytochrome c. Deuterium 14-23 cytochrome c, somatic Homo sapiens 71-83 11673874-8 2001 Interestingly, the deuterium isotope effect was decreased in the cytochrome c reductase assay with both nNOS and nNOSred when the assays were conducted in high ionic strength buffer, suggesting an increase in the rate of hydride transfer to FAD. Deuterium 19-28 cytochrome c, somatic Homo sapiens 65-77 11456893-0 2001 Direct observation of protein vibrations by selective incorporation of spectroscopically observable carbon-deuterium bonds in cytochrome c. Deuterium 107-116 cytochrome c, somatic Homo sapiens 126-138 22054221-5 2011 MALDI ISD analysis of deuterated cytochrome c yielded an extensive series of c-fragment ions which originate from cleavage of nearly all N-C(alpha) bonds (Cys17 to Glu104) allowing for a detailed analysis of the deuterium content of the backbone amides. Deuterium 212-221 cytochrome c, somatic Homo sapiens 33-45 22054221-6 2011 While hydrogen scrambling can be major concern when using mass spectrometric fragmentation to obtain detailed information on protein hydrogen exchange, we show that the level of hydrogen scrambling in our MALDI ISD measurements is negligible and that the known dynamic behavior of cytochrome c in solution is accurately reflected in the deuterium contents of the fragment ions. Deuterium 337-346 cytochrome c, somatic Homo sapiens 281-293 18781714-0 2008 Effect of deuterium substitution on electron transfer at cytochrome c/SAM interfaces. Deuterium 10-19 cytochrome c, somatic Homo sapiens 57-69 18381619-3 2008 Here we investigate the effects of electrospray capillary temperature on deuterium retention in backbone amides of various pepsin-generated cytochrome c peptides. Deuterium 73-82 cytochrome c, somatic Homo sapiens 140-152 16406808-5 2006 Partially deuterated cytochrome c peptides also lost more deuterium in UPLC versus HPLC, although the effect was not as pronounced as it was for the highly deuterated model peptides. Deuterium 58-67 cytochrome c, somatic Homo sapiens 21-33