PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16411679-4 2006 The Mo site of sulfite oxidase has two oxygen and three Mo-S ligands (two from cofactor dithiolene plus a cysteine). Oxygen 39-45 sulfite oxidase Homo sapiens 15-30 34915296-6 2022 The catalytic mechanism of the NADH oxidase mimics is that O2 involves in the oxidation of NADH, to generate O2.- intermediate and finally turn to H2O2, while SuOx mimics comes from that MoS2 particles can effectively catalyze sulfite to reduce (Fe(CN)6)3-. Oxygen 109-111 sulfite oxidase Homo sapiens 159-163 12148977-0 2002 Active-site stereochemical control of oxygen atom transfer reactivity in sulfite oxidase. Oxygen 38-44 sulfite oxidase Homo sapiens 73-88 31583830-0 2019 Oxygen Vacancy-Engineered PEGylated MoO3 -x Nanoparticles with Superior Sulfite Oxidase Mimetic Activity for Vitamin B1 Detection. Oxygen 0-6 sulfite oxidase Homo sapiens 72-87 4016147-8 1985 The O2 consumption of liver tissue and hepatocytes is significantly increased by sulfite due to the high activities of sulfite oxidase. Oxygen 4-6 sulfite oxidase Homo sapiens 119-134 32851830-4 2020 Oxygen atom transfer (OAT) reactivity is discussed in terms of breaking strong metal-oxo bonds and the mechanism of OAT catalyzed by enzymes of the sulfite oxidase (SO) family that possess dioxo Mo(VI) active sites. Oxygen 0-6 sulfite oxidase Homo sapiens 148-163 32851830-4 2020 Oxygen atom transfer (OAT) reactivity is discussed in terms of breaking strong metal-oxo bonds and the mechanism of OAT catalyzed by enzymes of the sulfite oxidase (SO) family that possess dioxo Mo(VI) active sites. Oxygen 0-6 sulfite oxidase Homo sapiens 165-167 31583830-3 2019 Herein, a SuOx mimic nanozyme of PEGylated (polyethylene glycol)-MoO3 -x nanoparticles (P-MoO3 -x NPs) with abundant oxygen vacancies created by vacancy-engineering is reported. Oxygen 117-123 sulfite oxidase Homo sapiens 10-14 26171830-0 2015 Oxygen reactivity of mammalian sulfite oxidase provides a concept for the treatment of sulfite oxidase deficiency. Oxygen 0-6 sulfite oxidase Homo sapiens 31-46 26171830-3 2015 In contrast, plant SO (PSO) lacks the haem domain and electrons shuttle from Moco to molecular oxygen. Oxygen 95-101 sulfite oxidase Homo sapiens 19-21 26171830-5 2015 In the present study, we generated mammalian haem-deficient and truncated SO variants and demonstrated their oxygen reactivity by hydrogen peroxide formation and oxygen-consumption studies. Oxygen 109-115 sulfite oxidase Homo sapiens 74-76 26171830-5 2015 In the present study, we generated mammalian haem-deficient and truncated SO variants and demonstrated their oxygen reactivity by hydrogen peroxide formation and oxygen-consumption studies. Oxygen 162-168 sulfite oxidase Homo sapiens 74-76 26171830-6 2015 We found that intramolecular electron transfer between Moco and haem showed an inverse correlation to SO oxygen reactivity. Oxygen 105-111 sulfite oxidase Homo sapiens 102-104 26171830-7 2015 Haem-deficient SO variants exhibited oxygen-dependent sulfite oxidation similar to PSO, which was confirmed further using haem-deficient human SO in a cell-based assay. Oxygen 37-43 sulfite oxidase Homo sapiens 15-17 26171830-9 2015 Therefore we evaluated the potential use of PEG attachment (PEGylation) as a modification method for future enzyme substitution therapies using oxygen-reactive SO variants, which might use blood-dissolved oxygen as the electron acceptor. Oxygen 144-150 sulfite oxidase Homo sapiens 160-162 26171830-9 2015 Therefore we evaluated the potential use of PEG attachment (PEGylation) as a modification method for future enzyme substitution therapies using oxygen-reactive SO variants, which might use blood-dissolved oxygen as the electron acceptor. Oxygen 205-211 sulfite oxidase Homo sapiens 160-162 25267303-6 2015 In examples of the SUOX-fold and DMSOR-fold enzymes, we observe three types of histidine-containing charge-transfer relays that can: (1) connect the piperazine ring of the pyranopterin to the substrate-binding site (SUOX-fold enzymes); (2) provide inter-pyranopterin communication (DMSOR-fold enzymes); and (3) connect a pyran ring oxygen to deeply buried water molecules (the DMSOR-fold NarGHI-type nitrate reductases). Oxygen 332-338 sulfite oxidase Homo sapiens 19-23 25267303-6 2015 In examples of the SUOX-fold and DMSOR-fold enzymes, we observe three types of histidine-containing charge-transfer relays that can: (1) connect the piperazine ring of the pyranopterin to the substrate-binding site (SUOX-fold enzymes); (2) provide inter-pyranopterin communication (DMSOR-fold enzymes); and (3) connect a pyran ring oxygen to deeply buried water molecules (the DMSOR-fold NarGHI-type nitrate reductases). Oxygen 332-338 sulfite oxidase Homo sapiens 216-220 25372012-1 2014 There are three families of mononuclear molybdenum enzymes that catalyze oxygen atom transfer (OAT) reactions, named after a typical example from each family, viz., dimethyl sulfoxide reductase (DMSOR), sulfite oxidase (SO), and xanthine oxidase (XO). Oxygen 73-79 sulfite oxidase Homo sapiens 203-218 25372012-1 2014 There are three families of mononuclear molybdenum enzymes that catalyze oxygen atom transfer (OAT) reactions, named after a typical example from each family, viz., dimethyl sulfoxide reductase (DMSOR), sulfite oxidase (SO), and xanthine oxidase (XO). Oxygen 73-79 sulfite oxidase Homo sapiens 197-199 23144459-3 2012 Low steady-state levels of H(2)S appear to be controlled primarily by efficient oxygen-dependent catabolism via sulfide quinone oxidoreductase, persulfide dioxygenase (ETHE1), rhodanese, and sulfite oxidase. Oxygen 80-86 sulfite oxidase Homo sapiens 191-206 23392406-3 2013 Sulfite biosensors are based on measurement of either O2 or electrons generated from splitting of H2O2 or heat released during oxidation of sulfite by immobilized sulfite oxidase. Oxygen 54-56 sulfite oxidase Homo sapiens 163-178