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PubMed:8288555 JSONTXT

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sentences

Id Subject Object Predicate Lexical cue
T1 0-28 Sentence denotes Heme-heme oxygenase complex.
T2 29-103 Sentence denotes Structure of the catalytic site and its implication for oxygen activation.
T3 104-373 Sentence denotes Heme oxygenase, a central monooxygenase enzyme of the heme catabolism and the associated generation of carbon monoxide, forms a 1:1 stoichiometric complex with iron protoporphyrin IX, which is a prosthetic active center and at the same time the substrate of the enzyme.
T4 374-530 Sentence denotes By using EPR, resonance Raman, and optical absorption spectroscopic techniques, we have determined the axial ligand coordination of the enzyme-heme complex.
T5 531-683 Sentence denotes The ferric heme iron in the heme-enzyme complex at neutral pH is six-coordinate high spin, while at alkaline pH (pKa 7.6), the complex becomes low spin.
T6 684-884 Sentence denotes Spectra of ferrous forms of the complex indicate that histidine serves as the iron proximal axial ligand and that the residue is in its neutral imidazole rather than its imidazolate protonation state.
T7 885-1062 Sentence denotes Thus, the active site of the heme-heme oxygenase complex has a myoglobin-like structure rather than an active site similar to the large cytochrome P-450 class of monooxygenases.
T8 1063-1273 Sentence denotes As a consequence, the activated form of the heme-heme oxygenase complex, a peroxo intermediate, is different from that of the cytochrome P-450 monooxygenases, in which the activated form is an oxo intermediate.
T9 1274-1443 Sentence denotes The overall catalytic mechanism is probably more closely related to that of other monooxygenases with myoglobin-like active sites, such as secondary amine monooxygenase.
T1 0-28 Sentence denotes Heme-heme oxygenase complex.
T2 29-103 Sentence denotes Structure of the catalytic site and its implication for oxygen activation.
T3 104-373 Sentence denotes Heme oxygenase, a central monooxygenase enzyme of the heme catabolism and the associated generation of carbon monoxide, forms a 1:1 stoichiometric complex with iron protoporphyrin IX, which is a prosthetic active center and at the same time the substrate of the enzyme.
T4 374-530 Sentence denotes By using EPR, resonance Raman, and optical absorption spectroscopic techniques, we have determined the axial ligand coordination of the enzyme-heme complex.
T5 531-683 Sentence denotes The ferric heme iron in the heme-enzyme complex at neutral pH is six-coordinate high spin, while at alkaline pH (pKa 7.6), the complex becomes low spin.
T6 684-884 Sentence denotes Spectra of ferrous forms of the complex indicate that histidine serves as the iron proximal axial ligand and that the residue is in its neutral imidazole rather than its imidazolate protonation state.
T7 885-1062 Sentence denotes Thus, the active site of the heme-heme oxygenase complex has a myoglobin-like structure rather than an active site similar to the large cytochrome P-450 class of monooxygenases.
T8 1063-1273 Sentence denotes As a consequence, the activated form of the heme-heme oxygenase complex, a peroxo intermediate, is different from that of the cytochrome P-450 monooxygenases, in which the activated form is an oxo intermediate.
T9 1274-1443 Sentence denotes The overall catalytic mechanism is probably more closely related to that of other monooxygenases with myoglobin-like active sites, such as secondary amine monooxygenase.

Glycosmos6-MAT

Id Subject Object Predicate Lexical cue
T1 767-775 http://purl.obolibrary.org/obo/MAT_0000491 denotes proximal

Anatomy-MAT

Id Subject Object Predicate Lexical cue mat_id
T1 767-775 Body_part denotes proximal http://purl.obolibrary.org/obo/MAT_0000491